2fym: Difference between revisions

Revision as of 11:00, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2fym.png

Template:STRUCTURE 2fym

Crystal structure of E. coli enolase complexed with the minimal binding segment of RNase E.Crystal structure of E. coli enolase complexed with the minimal binding segment of RNase E.

Template:ABSTRACT PUBMED 16516921

About this StructureAbout this Structure

2FYM is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Recognition of enolase in the Escherichia coli RNA degradosome., Chandran V, Luisi BF, J Mol Biol. 2006 Apr 21;358(1):8-15. Epub 2006 Feb 21. PMID:16516921

Page seeded by OCA on Tue Jul 29 11:00:38 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2fym.gif|left|200px]]
+{{Seed}}
+[[Image:2fym.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2fym|  PDB=2fym  |  SCENE=  }}
-'''Crystal structure of E. coli enolase complexed with the minimal binding segment of RNase E.'''
+===Crystal structure of E. coli enolase complexed with the minimal binding segment of RNase E.===
-==Overview==
+<!--
-In Escherichia coli, the glycolytic enzyme enolase is a component of the RNA degradosome, which is an RNase E mediated assembly involved in RNA processing and transcript turnover. The recruitment of enolase by the RNA degradosome has been implicated in the turnover of certain transcripts, and it is mediated by a small segment of roughly a dozen residues that lie within a natively unstructured sub-domain of RNase E. Here, we present the crystal structure of enolase in complex with its recognition site from RNase E at 1.6A resolution. A single molecule of the RNase E peptide binds asymmetrically in a conserved cleft at the interface of the enolase dimer. The recognition site is well conserved in RNase E homologues in a subfamily of the gamma-proteobacteria, including enzymes from pathogens such as Yersinia pestis, Vibrio cholera and Salmonella sp. We suggest that enolase is recruited into putative RNA degradosome machinery in these bacilli, where it plays common regulatory functions.
+The line below this paragraph, {{ABSTRACT_PUBMED_16516921}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16516921 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16516921}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Rna degradosome]]
 [[Category: Rnase e]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:27:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:00:38 2008''