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Structure of a putative NTP pyrophosphohydrolase: YP_001813558.1 from Exiguobacterium sibiricum 255-15
- Source :
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10
- Publication Year :
- 2010
-
Abstract
- The crystal structure of a putative NTP pyrophosphohydrolase, YP_001813558.1 from E. sibiricum, reveals a novel segment-swapped linked-dimer assembly.<br />The crystal structure of a putative NTPase, YP_001813558.1 from Exiguo­bacterium sibiricum 255-15 (PF09934, DUF2166) was determined to 1.78 Å resolution. YP_001813558.1 and its homologs (dimeric dUTPases, MazG proteins and HisE-encoded phosphoribosyl ATP pyrophosphohydrolases) form a superfamily of all-α-helical NTP pyrophosphatases. In dimeric dUTPase-like proteins, a central four-helix bundle forms the active site. However, in YP_001813558.1, an unexpected intertwined swapping of two of the helices that compose the conserved helix bundle results in a ‘linked dimer’ that has not previously been observed for this family. Interestingly, despite this novel mode of dimerization, the metal-binding site for divalent cations, such as magnesium, that are essential for NTPase activity is still conserved. Furthermore, the active-site residues that are involved in sugar binding of the NTPs are also conserved when compared with other α-helical NTPases, but those that recognize the nucleotide bases are not conserved, suggesting a different substrate specificity.
- Subjects :
- Models, Molecular
viruses
Dimer
Crystallography, X-Ray
Biochemistry
putative NTP pyrophosphohydrolase
chemistry.chemical_compound
Structural Biology
Models
Pyrophosphatases
Peptide sequence
chemistry.chemical_classification
Helix bundle
0303 health sciences
Crystallography
biology
030302 biochemistry & molecular biology
MazG nucleotide pyrophosphohydrolase
Biological Sciences
Condensed Matter Physics
3. Good health
Protein Structure
1.1 Normal biological development and functioning
Molecular Sequence Data
Biophysics
Divalent
Structural genomics
Quaternary
03 medical and health sciences
dUTPases
Underpinning research
Hydrolase
Genetics
Amino Acid Sequence
Protein Structure, Quaternary
030304 developmental biology
Structural Homology
Bacillales
Protein
Prevention
Active site
Molecular
structural genomics
Protein Structure, Tertiary
chemistry
Structural Homology, Protein
Chemical Sciences
biology.protein
X-Ray
Protein Multimerization
Novel Variants of Known Folds and Function
Tertiary
Subjects
Details
- ISSN :
- 17443091
- Volume :
- 66
- Issue :
- Pt 10
- Database :
- OpenAIRE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Accession number :
- edsair.doi.dedup.....7d42f540df70dc95889263c7eb3337b9