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Structure paper

TitleN5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis.
Journal, issue, pagesBiochemistry, Vol. 46, Page 2842-2855, Year 2007
Publish dateAug 24, 2005 (structure data deposition date)
AuthorsHoskins, A.A. / Morar, M. / Kappock, T.J. / Mathews, I.I. / Zaugg, J.B. / Barder, T.E. / Peng, P. / Okamoto, A. / Ealick, S.E. / Stubbe, J.
External linksBiochemistry / PubMed:17298082
MethodsX-ray diffraction
Resolution1.8 - 2.31 Å
Structure data

PDB-2ate:
Structure of the complex of PurE with NitroAIR
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2nsh:
E. coli PurE H45Q mutant complexed with nitro-AIR
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2nsj:
E. coli PurE H45Q mutant complexed with CAIR
Method: X-RAY DIFFRACTION / Resolution: 2.31 Å

PDB-2nsl:
E. coli PurE H45N mutant complexed with CAIR
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-NIA:
((2R,3S,4R,5R)-5-(5-AMINO-4-NITRO-1H-IMIDAZOL-1-YL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL)METHYL DIHYDROGEN PHOSPHATE

ChemComp-HOH:
WATER

ChemComp-C2R:
5-AMINO-1-(5-O-PHOSPHONO-BETA-D-RIBOFURANOSYL)-1H-IMIDAZOLE-4-CARBOXYLIC ACID

Source
  • escherichia coli (E. coli)
KeywordsLYASE / PurE / nitroAIR complex / central three-layer alpha-beta-alpha sandwich / kinked C-terminal helix / central three layer alpha-beta-alpha sandwich

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