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Structure paper

TitleBacillus cereus Phosphopentomutase Is an Alkaline Phosphatase Family Member That Exhibits an Altered Entry Point into the Catalytic Cycle.
Journal, issue, pagesJ. Biol. Chem., Vol. 286, Page 8043-8054, Year 2011
Publish dateMar 19, 2010 (structure data deposition date)
AuthorsPanosian, T.D. / Nannemann, D.P. / Watkins, G.R. / Phelan, V.V. / McDonald, W.H. / Wadzinski, B.E. / Bachmann, B.O. / Iverson, T.M.
External linksJ. Biol. Chem. / PubMed:21193409
MethodsX-ray diffraction
Resolution1.75 - 2.1 Å
Structure data

PDB-3m8w:
Phosphopentomutase from Bacillus cereus
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-3m8y:
Phosphopentomutase from Bacillus cereus after glucose-1,6-bisphosphate activation
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-3m8z:
Phosphopentomutase from Bacillus cereus bound with ribose-5-phosphate
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3ot9:
Phosphopentomutase from Bacillus cereus bound to glucose-1,6-bisphosphate
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-HSX:
5-O-phosphono-alpha-D-ribofuranose

ChemComp-G16:
1,6-di-O-phosphono-alpha-D-glucopyranose

Source
  • bacillus cereus (bacteria)
  • bacillus cereus (strain atcc 14579 / dsm 31 / jcm 2152 / nbrc 15305 / ncimb 9373 / nrrl b-3711) (bacteria)
KeywordsISOMERASE / alkaline phosphatase like core domain / di-metallo catalytic center / manganese binding / manganese / metal-binding / phosphopentomutase / ribose-5-phosphate / ribose-1-phosphate / glucose-1 / 6-bisphosphate / phosphoryl transfer

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