1b0k: Difference between revisions

Revision as of 17:59, 30 June 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:1b0k.png

Template:STRUCTURE 1b0k

S642A:FLUOROCITRATE COMPLEX OF ACONITASES642A:FLUOROCITRATE COMPLEX OF ACONITASE

Template:ABSTRACT PUBMED 10631981

About this StructureAbout this Structure

1B0K is a Single protein structure of sequence from Sus scrofa. This structure supersedes the now removed PDB entry 1as9. Full crystallographic information is available from OCA.

ReferenceReference

The mechanism of aconitase: 1.8 A resolution crystal structure of the S642a:citrate complex., Lloyd SJ, Lauble H, Prasad GS, Stout CD, Protein Sci. 1999 Dec;8(12):2655-62. PMID:10631981

Page seeded by OCA on Mon Jun 30 17:59:12 2008

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OCA

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-'''S642A:FLUOROCITRATE COMPLEX OF ACONITASE'''
+===S642A:FLUOROCITRATE COMPLEX OF ACONITASE===
-==Overview==
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-The crystal structure of the S642A mutant of mitochondrial aconitase (mAc) with citrate bound has been determined at 1.8 A resolution and 100 K to capture this binding mode of substrates to the native enzyme. The 2.0 A resolution, 100 K crystal structure of the S642A mutant with isocitrate binding provides a control, showing that the Ser --&gt; Ala replacement does not alter the binding of substrates in the active site. The aconitase mechanism requires that the intermediate product, cis-aconitate, flip over by 180 degrees about the C alpha-C beta double bond. Only one of these two alternative modes of binding, that of the isocitrate mode, has been previously visualized. Now, however, the structure revealing the citrate mode of binding provides direct support for the proposed enzyme mechanism.
+The line below this paragraph, {{ABSTRACT_PUBMED_10631981}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_10631981}}
 ==About this Structure==
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 [[Category: Transit peptide]]
 [[Category: Tricarboxylic acid cycle]]
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