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| | {{STRUCTURE_1ebh| PDB=1ebh | SCENE= }} | | {{STRUCTURE_1ebh| PDB=1ebh | SCENE= }} |
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| - | '''OCTAHEDRAL COORDINATION AT THE HIGH AFFINITY METAL SITE IN ENOLASE; CRYSTALLOGRAPHIC ANALYSIS OF THE MG++-ENZYME FROM YEAST AT 1.9 ANGSTROMS RESOLUTION'''
| + | ===OCTAHEDRAL COORDINATION AT THE HIGH AFFINITY METAL SITE IN ENOLASE; CRYSTALLOGRAPHIC ANALYSIS OF THE MG++-ENZYME FROM YEAST AT 1.9 ANGSTROMS RESOLUTION=== |
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| - | ==Overview==
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| - | The structure of the Mg2+ complex of yeast enolase has been determined from crystals grown in solutions of poly(ethylene glycol) at pH 8.1. Crystals belong to the space group P2(1) and have unit cell dimensions a = 72.5 A, b = 73.2 A, c = 89.1 A, and beta = 104.4 degrees. There is one dimer in the asymmetric unit. The current crystallographic R-factor is 19.0% for all recorded data to 1.9 A resolution. The electron density indicates a hexacoordinate Mg2+ at the high-affinity cation binding site. The octahedral coordination sphere consists of a meridional arrangement of three carboxylate oxygens from the side chains of Asp 246, Asp 320, and Glu 295, and three well-ordered water molecules. Octahedral coordination is the preferred geometry for alkaline earth metal ions in complexes with oxygen donor groups. In previous crystallographic studies of enolase, Zn2+ and Mg2+ complexes at the high-affinity site were reported to exist in trigonal bipyramidal coordination. This geometry was suggested to enhance the electrophilicity of the metal ion and promote rapid ligand exchange [Lebioda, L., & Stec, B. (1989) J. Am. Chem. Soc. 111, 8511-8513]. The octahedral arrangement of carboxylate and water ligands in the MgII-enolase complex determined here is most consistent with reports of the Mn2+ and Mg2+ coordination complexes of mandelate racemase and muconate lactonizing enzyme. These latter enzymes have alpha/beta-barrel folds comparable to enolase.(ABSTRACT TRUNCATED AT 250 WORDS) | + | The line below this paragraph, {{ABSTRACT_PUBMED_7703246}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 7703246 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_7703246}} |
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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 14:54:17 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:27:21 2008'' |
Revision as of 21:27, 30 June 2008
Template:STRUCTURE 1ebh
OCTAHEDRAL COORDINATION AT THE HIGH AFFINITY METAL SITE IN ENOLASE; CRYSTALLOGRAPHIC ANALYSIS OF THE MG++-ENZYME FROM YEAST AT 1.9 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 7703246
About this Structure
1EBH is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Octahedral coordination at the high-affinity metal site in enolase: crystallographic analysis of the MgII--enzyme complex from yeast at 1.9 A resolution., Wedekind JE, Reed GH, Rayment I, Biochemistry. 1995 Apr 4;34(13):4325-30. PMID:7703246
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