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TitleChelation of serine 39 to Mg2+ latches a gate at the active site of enolase: structure of the bis(Mg2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1-A resolution.
Journal, issue, pagesBiochemistry, Vol. 33, Page 9333-9342, Year 1994
Publish dateApr 27, 1994 (structure data deposition date)
AuthorsWedekind, J.E. / Poyner, R.R. / Reed, G.H. / Rayment, I.
External linksBiochemistry / PubMed:8049235
MethodsX-ray diffraction
Resolution2.1 Å
Structure data

PDB-1ebg:
CHELATION OF SER 39 TO MG2+ LATCHES A GATE AT THE ACTIVE SITE OF ENOLASE: STRUCTURE OF THE BIS(MG2+) COMPLEX OF YEAST ENOLASE AND THE INTERMEDIATE ANALOG PHOSPHONOACETOHYDROXAMATE AT 2.1 ANGSTROMS RESOLUTION
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-PAH:
PHOSPHONOACETOHYDROXAMIC ACID

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsCARBON-OXYGEN LYASE

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