2fym: Difference between revisions

Revision as of 18:26, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

2FYM is a Protein complex structure of sequences from Escherichia coli with as ligand. Active as Phosphopyruvate hydratase, with EC number 4.2.1.11 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 Thu Feb 21 17:26:25 2008

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OCA

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-[[Image:2fym.gif|left|200px]]<br /><applet load="2fym" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2fym.gif|left|200px]]<br /><applet load="2fym" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2fym, resolution 1.60&Aring;" />
 '''Crystal structure of E. coli enolase complexed with the minimal binding segment of RNase E.'''<br />
 ==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.
+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.
 ==About this Structure==
-FYM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FYM OCA].
+FYM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYM OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Protein complex]]
 [[Category: Chandran, V.]]
-[[Category: Luisi, B.F.]]
+[[Category: Luisi, B F.]]
 [[Category: MG]]
 [[Category: enolase]]
@@ Line 21: / Line 21: @@
 [[Category: rnase e]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:50:36 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:26:25 2008''