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Crystal structure of a bicupin protein HutD involved in histidine utilization in Pseudomonas.
- Source :
-
Proteins [Proteins] 2017 Aug; Vol. 85 (8), pp. 1580-1588. Date of Electronic Publication: 2017 Apr 25. - Publication Year :
- 2017
-
Abstract
- Cupins form one of the most functionally diverse superfamilies of proteins, with members performing a wide range of catalytic, non-catalytic, and regulatory functions. HutD is a predicted bicupin protein that is involved in histidine utilization (Hut) in Pseudomonas species. Previous genetic analyses have suggested that it limits the upper level of Hut pathway expression, but its mechanism of action is unknown. Here, we have determined the structure of PfluHutD at 1.74 Å resolution in several crystallization conditions, and identified N-formyl-l-glutamate (FG, a Hut pathway intermediate) as a potential ligand in vivo. Proteins 2017; 85:1580-1588. © 2017 Wiley Periodicals, Inc.<br /> (© 2017 Wiley Periodicals, Inc.)
- Subjects :
- Amino Acid Motifs
Bacterial Proteins genetics
Bacterial Proteins metabolism
Binding Sites
Biological Transport
Cloning, Molecular
Crystallography, X-Ray
Escherichia coli genetics
Escherichia coli metabolism
Gene Expression
Glutamates metabolism
Histidine metabolism
Models, Molecular
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Pseudomonas fluorescens metabolism
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins metabolism
Bacterial Proteins chemistry
Glutamates chemistry
Histidine chemistry
Pseudomonas fluorescens chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1097-0134
- Volume :
- 85
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- Proteins
- Publication Type :
- Academic Journal
- Accession number :
- 28383128
- Full Text :
- https://doi.org/10.1002/prot.25303