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TitleCrystal structure of Bacillus fastidious uricase reveals an unexpected folding of the C-terminus residues crucial for thermostability under physiological conditions.
Journal, issue, pagesAppl. Microbiol. Biotechnol., Vol. 99, Page 7973-7986, Year 2015
Publish dateSep 3, 2014 (structure data deposition date)
AuthorsFeng, J. / Wang, L. / Liu, H. / Yang, X. / Liu, L. / Xie, Y. / Liu, M. / Zhao, Y. / Li, X. / Wang, D. ...Feng, J. / Wang, L. / Liu, H. / Yang, X. / Liu, L. / Xie, Y. / Liu, M. / Zhao, Y. / Li, X. / Wang, D. / Zhan, C.G. / Liao, F.
External linksAppl. Microbiol. Biotechnol. / PubMed:25786739
MethodsX-ray diffraction
Resolution1.401 - 1.8 Å
Structure data

PDB-4r8x:
Crystal structure of a uricase from Bacillus fastidious
Method: X-RAY DIFFRACTION / Resolution: 1.401 Å

PDB-4r99:
Crystal structure of a uricase from Bacillus fastidious
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

Source
  • bacillus fastidiosus (bacteria)
KeywordsHYDROLASE / Bacillus fastidious uricase / fold / stability

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