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| | {{STRUCTURE_1ebg| PDB=1ebg | SCENE= }} | | {{STRUCTURE_1ebg| PDB=1ebg | SCENE= }} |
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| - | '''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'''
| + | ===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=== |
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| - | ==Overview==
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| - | The structure of a new crystal form of enolase from bakers' yeast has been solved to 2.1-A resolution. Crystals were grown from poly(ethylene glycol) and KCl at pH 8.2 in the presence of Mg2+ and a reaction intermediate analog, phosphonoacetohydroxamate (PhAH). Crystals belong to space group C2; have unit cell dimensions a = 123.5 A, b = 73.9 A, and c = 94.8 A with beta = 93.3 degrees; and contain one dimer per asymmetric unit. The structure was solved by molecular replacement from the X-ray coordinates of apoenolase [Stec, B., & Lebioda, L. (1990) J. Mol. Biol. 211, 235-248]. Both essential divalent metal ions are observed to be complexed with the inhibitor. The two Mg2+ ions are 4.05 A apart and are bridged by a mu-oxyl ligand from the carbonyl moiety of PhAH. The "high-affinity" Mg2+ coordinates to the carboxylate side chains of Asp 246, Glu 295, and Asp 320, one water molecule, and the hydroxamate and carbonyl oxygens of PhAH. The second Mg2+ coordinates to a phosphonyl oxygen, two water molecules, and the mu-bridge carbonyl oxygen of PhAH. Coordination schemes with respect to PhAH and water ligands are fully consistent with those of the Mn2+ complexes determined spectroscopically [Poyner, R.R., & Reed, G. H. (1992) Biochemistry 31, 7166-7173]. Remaining ligands for the second Mg2+ are the carbonyl oxygen and gamma-oxygen of Ser 39. Chelation of this Ser residue to Mg2+ effectively "latches" a flexible loop extending from Gly 37 through His 43 and closes off the entrance to the active site. The position of the second Mg2+ in the active site provides new insight into the stereochemistry of substrate binding. | + | The line below this paragraph, {{ABSTRACT_PUBMED_8049235}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8049235 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8049235}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Wedekind, J E.]] | | [[Category: Wedekind, J E.]] |
| | [[Category: Carbon-oxygen lyase]] | | [[Category: Carbon-oxygen lyase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:54:19 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:27:16 2008'' |
Revision as of 21:27, 30 June 2008
Template:STRUCTURE 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
Template:ABSTRACT PUBMED 8049235
About this Structure
1EBG is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Chelation 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., Wedekind JE, Poyner RR, Reed GH, Rayment I, Biochemistry. 1994 Aug 9;33(31):9333-42. PMID:8049235
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