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

Journal Article · · Acta Crystallographica. Section F
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  1. The Scripps Research Institute, La Jolla, CA (United States). Joint Center for Structural Genomics; The Scripps Research Institute, La Jolla, CA (United States). Dept. of Molecular Biology; DOE/OSTI
  2. The Scripps Research Institute, La Jolla, CA (United States). Joint Center for Structural Genomics; The Scripps Research Institute, La Jolla, CA (United States). Dept. of Molecular Biology
  3. Univ. of California, Los Angeles, CA (United States). Dept. of Chemistry and Biochemistry
  4. The Scripps Research Institute, La Jolla, CA (United States). Joint Center for Structural Genomics; SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
  5. MRC Laboratory of Molecular Biology, Cambridge (United States)
  6. The Scripps Research Institute, La Jolla, CA (United States). Joint Center for Structural Genomics; Univ. of California, San Diego, La Jolla, CA (United States). Center for Reseach in Biological Systems; Sanford–Burnham Medical Research Institute, La Jolla, CA (United States). Program on Bioinformatics and Systems Biology
  7. The Scripps Research Institute, La Jolla, CA (United States). Joint Center for Structural Genomics; Genomics Institute of the Novartis Research Foundation, San Diego, CA (United States). Protein Sciences Dept.
  8. The Scripps Research Institute, La Jolla, CA (United States). Joint Center for Structural Genomics; Univ. of California, San Diego, La Jolla, CA (United States). Center for Reseach in Biological Systems
  9. The Scripps Research Institute, La Jolla, CA (United States). Joint Center for Structural Genomics; Univ. of California, San Diego, La Jolla, CA (United States). Center for Research in Biological Systems
  10. The Scripps Research Institute, La Jolla, CA (United States). Joint Center for Structural Genomics; Sanford–Burnham Medical Research Institute, La Jolla, CA (United States). Program on Bioinformatics and Systems Biology
  11. The Scripps Research Institute, La Jolla, CA (United States). Joint Center for Structural Genomics; SLAC National Accelerator Lab., Menlo Park, CA (United States). Photon Science
  12. The Scripps Research Institute, La Jolla, CA (United States). Joint Center for Structural Genomics; Univ. of California, San Diego, La Jolla, CA (United States). Center for Research in Biological Systems; Sanford–Burnham Medical Research Institute, La Jolla, CA (United States). Program on Bioinformatics and Systems Biology
  13. The Scripps Research Institute, La Jolla, CA (United States). Joint Center for Structural Genomics; The Scripps Research Inst., La Jolla, CA (United States). Dept. of Molecular Biology; Genomics Institute of the Novartis Research Foundation, San Diego, CA (United States). Protein Sciences Dept.
  14. The Scripps Research Institute, La Jolla, CA (United States). Joint Center for Structural Genomics; The Scripps Research Inst., La Jolla, CA (United States). Dept. of Molecular Biology
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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--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 activesite residues that are involved in sugar binding of the NTPs are also conserved when compared with other -helical NTPases, but those that recognize the nucleotide bases are not conserved, suggesting a different substrate specificity.
Research Organization:
Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division
Grant/Contract Number:
AC02-05CH11231
OSTI ID:
1625802
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: 10 Vol. 66; ISSN ACSFCL; ISSN 1744-3091
Publisher:
International Union of CrystallographyCopyright Statement
Country of Publication:
United States
Language:
English

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
Biochemistry & Molecular Biology
Biophysics
Crystallography