1ebh: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:1ebh.jpg|left|200px]]
{{Seed}}
[[Image:1ebh.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ebh|  PDB=1ebh  |  SCENE=  }}  
{{STRUCTURE_1ebh|  PDB=1ebh  |  SCENE=  }}  


'''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===




==Overview==
<!--
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., &amp; 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.
-->
{{ABSTRACT_PUBMED_7703246}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[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

File:1ebh.png

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

Page seeded by OCA on Tue Jul 1 00:27:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1ebh&oldid=591540"