Structure of a putative NTP pyrophosphohydrolase: YP_001813558.1 from Exiguobacterium sibiricum 255-15

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 a...

Full description

Saved in:
Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2010-10, Vol.66 (10), p.1237-1244
Main Authors: Han, Gye Won, Elsliger, Marc-André, Yeates, Todd O., Xu, Qingping, Murzin, Alexey G., Krishna, S. Sri, Jaroszewski, Lukasz, Abdubek, Polat, Astakhova, Tamara, Axelrod, Herbert L., Carlton, Dennis, Chen, Connie, Chiu, Hsiu-Ju, Clayton, Thomas, Das, Debanu, Deller, Marc C., Duan, Lian, Ernst, Dustin, Feuerhelm, Julie, Grant, Joanna C., Grzechnik, Anna, Jin, Kevin K., Johnson, Hope A., Klock, Heath E., Knuth, Mark W., Kozbial, Piotr, Kumar, Abhinav, Lam, Winnie W., Marciano, David, McMullan, Daniel, Miller, Mitchell D., Morse, Andrew T., Nigoghossian, Edward, Okach, Linda, Reyes, Ron, Rife, Christopher L., Sefcovic, Natasha, Tien, Henry J., Trame, Christine B., Van Den Bedem, Henry, Weekes, Dana, Hodgson, Keith O., Wooley, John, Deacon, Ashley M., Godzik, Adam, Lesley, Scott A., Wilson, Ian A.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacillales - enzymology
BASIC BIOLOGICAL SCIENCES
Binding
Biochemistry & Molecular Biology
Biophysics
Bundling
Crystal structure
Crystallography
Crystallography, X-Ray
Dimers
dUTPases
Magnesium
MazG nucleotide pyrophosphohydrolase
Models, Molecular
Molecular Sequence Data
Novel Variants of Known Folds and Function
Nucleotides
Protein Multimerization
Protein Structure, Quaternary
Protein Structure, Tertiary
Proteins
putative NTP pyrophosphohydrolase
Pyrophosphatases - chemistry
Residues
structural genomics
Structural Homology, Protein
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1744-3091
1744-3091
2053-230X
DOI:10.1107/S1744309110025534