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21 results on '"Vadlamani, Grishma"'

5. Solution NMR and racemic crystallography provide insights into a novel structural class of cyclic plant peptides

Author

Payne, Colton D., primary, Vadlamani, Grishma, additional, Hajiaghaalipour, Fatemeh, additional, Muhammad, Taj, additional, Fisher, Mark F., additional, Andersson, Håkan S., additional, Göransson, Ulf, additional, Clark, Richard J., additional, Bond, Charles S., additional, Mylne, Joshua S., additional, and Rosengren, K. Johan, additional

Published
2021
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7. Solution NMR and racemic crystallography provide insights into a novel structural class of cyclic plant peptides

Author

Payne, Colton D., Vadlamani, Grishma, Hajiaghaalipour, Fatemeh, Muhammad, Taj, Fisher, Mark F., Andersson, Håkan S., Göransson, Ulf, Clark, Richard J., Bond, Charles S., Mylne, Joshua S., Rosengren, K. Johan, Payne, Colton D., Vadlamani, Grishma, Hajiaghaalipour, Fatemeh, Muhammad, Taj, Fisher, Mark F., Andersson, Håkan S., Göransson, Ulf, Clark, Richard J., Bond, Charles S., Mylne, Joshua S., and Rosengren, K. Johan

Abstract

Head-to-tail cyclic and disulfide-rich peptides are natural products with applications in drug design. Among these are the PawS-Derived Peptides (PDPs) produced in seeds of the daisy plant family. PDP-23 is a unique member of this class in that it is twice the typical size and adopts two beta-hairpins separated by a hinge region. The beta-hairpins, both stabilised by a single disulfide bond, fold together into a V-shaped tertiary structure creating a hydrophobic core. In water two PDP-23 molecules merge their hydrophobic cores to form a square prism quaternary structure. Here, we synthesised PDP-23 and its enantiomer comprising d-amino acids and achiral glycine, which allowed us to confirm these solution NMR structural data by racemic crystallography. Furthermore, we discovered the related PDP-24. NMR analysis showed that PDP-24 does not form a dimeric structure and it has poor water solubility, but in less polar solvents adopts near identical secondary and tertiary structure to PDP-23. The natural role of these peptides in plants remains enigmatic, as we did not observe any antimicrobial or insecticidal activity. However, the plasticity of these larger PDPs and their ability to change structure under different conditions make them appealing peptide drug scaffolds.

Published
2021
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9. A chameleonic macrocyclic peptide with drug delivery applications

Author

Payne, Colton D., primary, Franke, Bastian, additional, Fisher, Mark F., additional, Hajiaghaalipour, Fatemeh, additional, McAleese, Courtney E., additional, Song, Angela, additional, Eliasson, Carl, additional, Zhang, Jingjing, additional, Jayasena, Achala S., additional, Vadlamani, Grishma, additional, Clark, Richard J., additional, Minchin, Rodney F., additional, Mylne, Joshua S., additional, and Rosengren, K. Johan, additional

Published
2021
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12. The structure of a conserved domain of TamB reveals a hydrophobic β taco fold

Author

Josts, Inokentijs, Stubenrauch, Christopher James, Vadlamani, Grishma, Mosbahi, Khedidja, Walker, Daniel, Lithgow, Trevor, and Grinter, Rhys

Abstract

The translocation and assembly module (TAM) plays a role in the transport and insertion of proteins into the bacterial outer membrane. TamB, a component of this system spans the periplasmic space to engage with its partner protein TamA. Despite efforts to characterize the TAM, the structure and mechanism of action of TamB remained enigmatic. Here we present the crystal structure of TamB amino acids 963-1,138. This region represents half of the conserved DUF490 domain, the defining feature of TamB. TamB963-1138 consists of a concave, taco-shaped β sheet with a hydrophobic interior. This β taco structure is of dimensions capable of accommodating and shielding the hydrophobic side of an amphipathic β strand, potentially allowing TamB to chaperone nascent membrane proteins from the aqueous environment. In addition, sequence analysis suggests that the structure of TamB963-1138 is shared by a large portion of TamB. This architecture could allow TamB to act as a conduit for membrane proteins.

Published
2017

13. Conformational flexibility of the glycosidase NagZ allows it to bind structurally diverse inhibitors to suppress β-lactam antibiotic resistance

Author

Tamigney Kenfack, Marielle, Mazur, Marcelina, Nualnoi, Teerapat, Shaffer, Teresa, Ngassimou, Abba, Marrot, Jérôme, Marchetti, Roberta, Sintiprungrat, Kitisak, Chantratita, Narisara, Silipo, Alba, Molinaro, Antonio, AuCoin, David, Burtnick, Mary, Brett, Paul, Gauthier, Charles, Vadlamani, Grishma, Stubbs, Keith, Desire, Jerome, Blériot, Yves, Vocadlo, David, Mark, Brian, Institut de Chimie des Milieux et Matériaux de Poitiers (IC2MP), Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université de Poitiers-Institut de Chimie du CNRS (INC), Wroclaw University of Environmental and Life Sciences, School of Medicine [Reno], University of Nevada [Reno], Institut Lavoisier de Versailles (ILV), Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Department of Chemical Sciences, University of Naples Federico II, Napoli, Italy, Mahidol University [Bangkok], Dipartimento di Scienze Chimiche, Complesso Universitario Monte Sant’Angelo, Università degli studi di Napoli Federico II, School of Molecular and Microbial Sciences, University of Queensland [Brisbane], Chimie Moléculaire de Paris Centre (FR 2769), Institut de Chimie du CNRS (INC)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-Université Pierre et Marie Curie - Paris 6 (UPMC), Simon Fraser University (SFU.ca), University of Manitoba [Winnipeg], Université de Poitiers-Institut national des sciences de l'Univers (INSU - CNRS)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), and Université Paris sciences et lettres (PSL)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[CHIM.CATA]Chemical Sciences/Catalysis, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2017

15. Synergistic activity of fosfomycin, β-lactams and peptidoglycan recycling inhibition againstPseudomonas aeruginosa

Author

Hamou-Segarra, Myriam, primary, Zamorano, Laura, additional, Vadlamani, Grishma, additional, Chu, Mitchell, additional, Sanchez-Diener, Irina, additional, Juan, Carlos, additional, Blazquez, Jesús, additional, Hattie, Mitchell, additional, Stubbs, Keith A., additional, Mark, Brian L., additional, and Oliver, Antonio, additional

Published
2016
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18. Crystal structure of Arabidopsis thalianaHPPK/DHPS, a bifunctional enzyme and target of the herbicide asulam

Author

Vadlamani, Grishma, Sukhoverkov, Kirill V., Haywood, Joel, Breese, Karen J., Fisher, Mark F., Stubbs, Keith A., Bond, Charles S., and Mylne, Joshua S.

Abstract

Herbicides are vital for modern agriculture, but their utility is threatened by genetic or metabolic resistance in weeds as well as regulatory barriers. Of the known herbicide modes of action, 7,8-dihydropterin synthase (DHPS) which is involved in folate biosynthesis, is targeted by just one commercial herbicide, asulam. A mimic of the substrate para-aminobenzoic acid, asulam is chemically similar to sulfonamide antibiotics – and while still in widespread use, asulam has faced regulatory scrutiny. With an entire mode of action represented by just one commercial agrochemical, we sought to improve the understanding of its plant target. Here we solve a 2.3 Å resolution crystal structure for Arabidopsis thalianaDHPS that is conjoined to 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) and reveal a strong structural conservation with bacterial counterparts at the sulfonamide-binding pocket of DHPS. We demonstrate asulam and the antibiotic sulfamethoxazole have herbicidal as well as antibacterial activity and explore the structural basis of their potency by modelling these compounds in mitochondrial HPPK/DHPS. Our findings suggest limited opportunity for the rational design of plant selectivity from asulam and that pharmacokinetic or delivery differences between plants and microbes might be the best ways to safeguard this mode of action.

Published
2022
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20. Solution NMR and racemic crystallography provide insights into a novel structural class of cyclic plant peptides.

Author

Payne CD, Vadlamani G, Hajiaghaalipour F, Muhammad T, Fisher MF, Andersson HS, Göransson U, Clark RJ, Bond CS, Mylne JS, and Rosengren KJ

Abstract

Head-to-tail cyclic and disulfide-rich peptides are natural products with applications in drug design. Among these are the PawS-Derived Peptides (PDPs) produced in seeds of the daisy plant family. PDP-23 is a unique member of this class in that it is twice the typical size and adopts two β-hairpins separated by a hinge region. The β-hairpins, both stabilised by a single disulfide bond, fold together into a V-shaped tertiary structure creating a hydrophobic core. In water two PDP-23 molecules merge their hydrophobic cores to form a square prism quaternary structure. Here, we synthesised PDP-23 and its enantiomer comprising d-amino acids and achiral glycine, which allowed us to confirm these solution NMR structural data by racemic crystallography. Furthermore, we discovered the related PDP-24. NMR analysis showed that PDP-24 does not form a dimeric structure and it has poor water solubility, but in less polar solvents adopts near identical secondary and tertiary structure to PDP-23. The natural role of these peptides in plants remains enigmatic, as we did not observe any antimicrobial or insecticidal activity. However, the plasticity of these larger PDPs and their ability to change structure under different conditions make them appealing peptide drug scaffolds., Competing Interests: The authors declare no conflicts of interest., (This journal is © The Royal Society of Chemistry.)

Published
2021
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21. The Structure of a Conserved Domain of TamB Reveals a Hydrophobic β Taco Fold.

Author

Josts I, Stubenrauch CJ, Vadlamani G, Mosbahi K, Walker D, Lithgow T, and Grinter R

Subjects
Amino Acid Motifs, Bacterial Outer Membrane Proteins metabolism, Escherichia coli Proteins metabolism, Hydrophobic and Hydrophilic Interactions, Protein Domains, Bacterial Outer Membrane Proteins chemistry, Conserved Sequence, Escherichia coli Proteins chemistry
Abstract

The translocation and assembly module (TAM) plays a role in the transport and insertion of proteins into the bacterial outer membrane. TamB, a component of this system spans the periplasmic space to engage with its partner protein TamA. Despite efforts to characterize the TAM, the structure and mechanism of action of TamB remained enigmatic. Here we present the crystal structure of TamB amino acids 963-1,138. This region represents half of the conserved DUF490 domain, the defining feature of TamB. TamB 963-1138 consists of a concave, taco-shaped β sheet with a hydrophobic interior. This β taco structure is of dimensions capable of accommodating and shielding the hydrophobic side of an amphipathic β strand, potentially allowing TamB to chaperone nascent membrane proteins from the aqueous environment. In addition, sequence analysis suggests that the structure of TamB 963-1138 is shared by a large portion of TamB. This architecture could allow TamB to act as a conduit for membrane proteins., (Copyright © 2017 The Authors. Published by Elsevier Ltd.. All rights reserved.)

Published
2017
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