1gh8: Difference between revisions

Revision as of 05:16, 1 July 2008

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File:1gh8.png

Template:STRUCTURE 1gh8

SOLUTION STRUCTURE OF THE ARCHAEAL TRANSLATION ELONGATION FACTOR 1BETA FROM METHANOBACTERIUM THERMOAUTOTROPHICUMSOLUTION STRUCTURE OF THE ARCHAEAL TRANSLATION ELONGATION FACTOR 1BETA FROM METHANOBACTERIUM THERMOAUTOTROPHICUM

Template:ABSTRACT PUBMED 10959626

About this StructureAbout this Structure

1GH8 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. This structure supersedes the now removed PDB entry 1d5k. Full experimental information is available from OCA.

ReferenceReference

Rapid fold and structure determination of the archaeal translation elongation factor 1beta from Methanobacterium thermoautotrophicum., Kozlov G, Ekiel I, Beglova N, Yee A, Dharamsi A, Engel A, Siddiqui N, Nong A, Gehring K, J Biomol NMR. 2000 Jul;17(3):187-94. PMID:10959626

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OCA

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-'''SOLUTION STRUCTURE OF THE ARCHAEAL TRANSLATION ELONGATION FACTOR 1BETA FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''
+===SOLUTION STRUCTURE OF THE ARCHAEAL TRANSLATION ELONGATION FACTOR 1BETA FROM METHANOBACTERIUM THERMOAUTOTROPHICUM===
-==Overview==
+<!--
-The tertiary fold of the elongation factor, aEF-1beta, from Methanobacterium thermoautotrophicum was determined in a high-throughput fashion using a minimal set of NMR experiments. NMR secondary structure prediction, deuterium exchange experiments and the analysis of chemical shift perturbations were combined to identify the protein fold as an alpha-beta sandwich typical of many RNA binding proteins including EF-G. Following resolution of the tertiary fold, a high resolution structure of aEF-1beta was determined using heteronuclear and homonuclear NMR experiments and a semi-automated NOESY assignment strategy. Analysis of the aEF-1beta structure revealed close similarity to its human analogue, eEF-1beta. In agreement with studies on EF-Ts and human EF-1beta, a functional mechanism for nucleotide exchange is proposed wherein Phe46 on an exposed loop acts as a lever to eject GDP from the associated elongation factor G-protein, aEF-1alpha. aEF-1beta was also found to bind calcium in the groove between helix alpha2 and strand beta4. This novel feature was not observed previously and may serve a structural function related to protein stability or may play a functional role in archaeal protein translation.
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+(as it appears on PubMed at http://www.pubmed.gov), where 10959626 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10959626}}
 ==About this Structure==
-GH8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1d5k 1d5k]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GH8 OCA].
+GH8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1d5k 1d5k]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GH8 OCA].
 ==Reference==
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 [[Category: Psi]]
 [[Category: Structural genomic]]
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