3h8a: Difference between revisions
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[[Image: | ==Crystal structure of E. coli enolase bound to its cognate RNase E recognition domain== | ||
<StructureSection load='3h8a' size='340' side='right' caption='[[3h8a]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3h8a]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H8A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H8A FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3h8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h8a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h8a RCSB], [http://www.ebi.ac.uk/pdbsum/3h8a PDBsum]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h8/3h8a_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In Escherichia coli and many other bacterial species, the glycolytic enzyme enolase is a component of the multi-enzyme RNA degradosome, an assembly that is involved in RNA processing and degradation. Enolase is recruited into the degradosome through interactions with a small recognition motif located within the degradosome-scaffolding domain of RNase E. Here, the crystal structure of enolase bound to its cognate site from RNase E (residues 823-850) at 1.9 A resolution is presented. The structure suggests that enolase may help to organize an adjacent conserved RNA-binding motif in RNase E. | |||
Molecular recognition between Escherichia coli enolase and ribonuclease E.,Nurmohamed S, McKay AR, Robinson CV, Luisi BF Acta Crystallogr D Biol Crystallogr. 2010 Sep;66(Pt 9):1036-40. Epub 2010 Aug 13. PMID:20823555<ref>PMID:20823555</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Enolase|Enolase]] | *[[Enolase|Enolase]] | ||
*[[Ribonuclease|Ribonuclease]] | |||
== | == References == | ||
< | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Phosphopyruvate hydratase]] | [[Category: Phosphopyruvate hydratase]] | ||
[[Category: Luisi, B F | [[Category: Luisi, B F]] | ||
[[Category: Nurmohamed, S | [[Category: Nurmohamed, S]] | ||
[[Category: Glycolytic enzyme]] | [[Category: Glycolytic enzyme]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
Revision as of 08:48, 8 December 2014
Crystal structure of E. coli enolase bound to its cognate RNase E recognition domain
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