2nu8: Difference between revisions

Revision as of 06:25, 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:2nu8.png

Template:STRUCTURE 2nu8

C123aT Mutant of E. coli Succinyl-CoA SynthetaseC123aT Mutant of E. coli Succinyl-CoA Synthetase

Template:ABSTRACT PUBMED 17642514

About this StructureAbout this Structure

2NU8 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Participation of Cys123alpha of Escherichia coli succinyl-CoA synthetase in catalysis., Hidber E, Brownie ER, Hayakawa K, Fraser ME, Acta Crystallogr D Biol Crystallogr. 2007 Aug;63(Pt 8):876-84. Epub 2007, Jul 17. PMID:17642514

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

OCA

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-'''C123aT Mutant of E. coli Succinyl-CoA Synthetase'''
+===C123aT Mutant of E. coli Succinyl-CoA Synthetase===
-==Overview==
+<!--
-Succinyl-CoA synthetase has a highly conserved cysteine residue, Cys123alpha in the Escherichia coli enzyme, that is located near the CoA-binding site and the active-site histidine residue. To test whether the succinyl moiety of succinyl-CoA is transferred to the thiol of Cys123alpha as part of the catalytic mechanism, this residue was mutated to alanine, serine, threonine and valine. Each mutant protein was catalytically active, although less active than the wild type. This proved that the specific formation of a thioester bond with Cys123alpha is not part of the catalytic mechanism. To understand why the mutations affected catalysis, the crystal structures of the four mutant proteins were determined. The alanine mutant showed no structural changes yet had reduced activity, suggesting that the size of the cysteine is important for optimal activity. These results explain why this cysteine residue is conserved in the sequences of succinyl-CoA synthetases from different sources.
+The line below this paragraph, {{ABSTRACT_PUBMED_17642514}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17642514}}
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 [[Category: Ligase]]
 [[Category: Rossmann fold]]
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