1e9i: Difference between revisions

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|PDB= 1e9i |SIZE=350|CAPTION= <scene name='initialview01'>1e9i</scene>, resolution 2.48&Aring;
|PDB= 1e9i |SIZE=350|CAPTION= <scene name='initialview01'>1e9i</scene>, resolution 2.48&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11]  
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </span>
|GENE= ENO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= ENO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9i OCA], [http://www.ebi.ac.uk/pdbsum/1e9i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e9i RCSB]</span>
}}
}}


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[[Category: Kuhnel, K.]]
[[Category: Kuhnel, K.]]
[[Category: Luisi, B.]]
[[Category: Luisi, B.]]
[[Category: MG]]
[[Category: SO4]]
[[Category: degradosome]]
[[Category: degradosome]]
[[Category: lyase]]
[[Category: lyase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:52:07 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:58:01 2008''

Revision as of 16:58, 30 March 2008

File:1e9i.jpg


Drag the structure with the mouse to rotate
1e9i, resolution 2.48Å
Ligands: MG, SO4
Gene: ENO (Escherichia coli)
Activity: Phosphopyruvate hydratase, with EC number 4.2.1.11
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



ENOLASE FROM E.COLI


Overview

The crystal structure of Escherichia coli enolase (EC 4.2.1.11, phosphopyruvate hydratase), which is a component of the RNA degradosome, has been determined at 2.5 A. There are four molecules in the asymmetric unit of the C2 cell, and in one of the molecules, flexible loops close onto the active site. This closure mimics the conformation of the substrate-bound intermediate. A comparison of the structure of the E. coli enolase with the eukaryotic enolase structures available (lobster and yeast) indicates a high degree of conservation of the hydrophobic core and the subunit interface of this homodimeric enzyme. The dimer interface is enriched in charged residues compared with other protein homodimers, which may explain our observations from analytical ultracentrifugation that dimerisation is affected by ionic strength. The putative role of enolase in the RNA degradosome is discussed; although it was not possible to ascribe a specific role to it, a structural role is possible.

About this Structure

1E9I is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of the Escherichia coli RNA degradosome component enolase., Kuhnel K, Luisi BF, J Mol Biol. 2001 Oct 26;313(3):583-92. PMID:11676541

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