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Structure paper

TitleStructure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products.
Journal, issue, pagesProtein Sci., Vol. 16, Page 1230-1235, Year 2007
Publish dateJan 10, 2007 (structure data deposition date)
AuthorsOlsen, L.R. / Vetting, M.W. / Roderick, S.L.
External linksProtein Sci. / PubMed:17473010
MethodsX-ray diffraction
Resolution2.2 - 2.54 Å
Structure data

PDB-2oi5:
E. coli GlmU- Complex with UDP-GlcNAc and Acetyl-CoA
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-2oi6:
E. coli GlmU- Complex with UDP-GlcNAc, CoA and GlcN-1-PO4
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-2oi7:
E. coli GlmU- Complex with UDP-GlcNAc, desulpho-CoA and GlcNAc-1-PO4
Method: X-RAY DIFFRACTION / Resolution: 2.54 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-ACO:
ACETYL COENZYME *A

ChemComp-UD1:
URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE

ChemComp-HOH:
WATER

ChemComp-GP1:
2-amino-2-deoxy-1-O-phosphono-alpha-D-glucopyranose

ChemComp-CO:
Unknown entry

ChemComp-COA:
COENZYME A

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

ChemComp-DCA:
DESULFO-COENZYME A

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / LEFT-HANDED BETA HELIX

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