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TitleStructure of the Bacterial Deacetylase LpxC Bound to the Nucleotide Reaction Product Reveals Mechanisms of Oxyanion Stabilization and Proton Transfer.
Journal, issue, pagesJ. Biol. Chem., Vol. 288, Page 34073-34080, Year 2013
Publish dateAug 23, 2013 (structure data deposition date)
AuthorsClayton, G.M. / Klein, D.J. / Rickert, K.W. / Patel, S.B. / Kornienko, M. / Zugay-Murphy, J. / Reid, J.C. / Tummala, S. / Sharma, S. / Singh, S.B. ...Clayton, G.M. / Klein, D.J. / Rickert, K.W. / Patel, S.B. / Kornienko, M. / Zugay-Murphy, J. / Reid, J.C. / Tummala, S. / Sharma, S. / Singh, S.B. / Miesel, L. / Lumb, K.J. / Soisson, S.M.
External linksJ. Biol. Chem. / PubMed:24108127
MethodsX-ray diffraction
Resolution2.59 Å
Structure data

PDB-4mdt:
Structure of LpxC bound to the reaction product UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine
Method: X-RAY DIFFRACTION / Resolution: 2.59 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-24G:
uridine-5'-diphosphate-3-O-(R-3-hydroxymyristoyl)-glucosamine

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / Deacetylase

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