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TitleCrystal structures identify an atypical two-metal-ion mechanism for uridyltransfer in GlmU: its significance to sugar nucleotidyl transferases
Journal, issue, pagesJ. Mol. Biol., Vol. 425, Page 1745-1759, Year 2013
Publish dateJul 22, 2012 (structure data deposition date)
AuthorsJagtap, P.K.A. / Verma, S.K. / Vithani, N. / Bais, V.S. / Prakash, B.
External linksJ. Mol. Biol. / PubMed:23485416
MethodsX-ray diffraction
Resolution2.03 - 2.6 Å
Structure data

PDB-4g87:
Crystal structure of GLMU from Mycobacterium tuberculosis snapshot 1
Method: X-RAY DIFFRACTION / Resolution: 2.03 Å

PDB-4hcq:
Crystal structure of GLMU from mycobacterium tuberculosis in complex with glucosamine-1-phosphate
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-CO:
Unknown entry

ChemComp-UD1:
URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE

ChemComp-POP:
PYROPHOSPHATE 2-

ChemComp-HOH:
WATER

ChemComp-GN1:
2-acetamido-2-deoxy-1-O-phosphono-alpha-D-glucopyranose

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsTRANSFERASE / ACETYLTRANSFERASE / BIFUNCTIONAL / PYROPHOSPHORYLASE / ROSSMANN-LIKE FOLD / LEFT-HANDED-BETA-HELIX / CELL SHAPE / CELL WALL BIOGENESIS/DEGRADATION / METAL-BINDING / MULTIFUNCTIONAL ENZYME / NUCLEOTIDYLTRANSFERASE / PEPTIDOGLYCAN SYNTHESIS / ACYLTRANSFERASE / MAGNESIUM

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