1c97: Difference between revisions

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[[Image:1c97.gif|left|200px]]
{{Seed}}
[[Image:1c97.png|left|200px]]


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{{STRUCTURE_1c97|  PDB=1c97  |  SCENE=  }}  
{{STRUCTURE_1c97|  PDB=1c97  |  SCENE=  }}  


'''S642A:ISOCITRATE COMPLEX OF ACONITASE'''
===S642A:ISOCITRATE 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==
==About this Structure==
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[[Category: Transit peptide]]
[[Category: Transit peptide]]
[[Category: Tricarboxylic acid cycle]]
[[Category: Tricarboxylic acid cycle]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:29:01 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:23:36 2008''

Revision as of 17:23, 30 June 2008

File:1c97.png

Template:STRUCTURE 1c97

S642A:ISOCITRATE COMPLEX OF ACONITASE

Template:ABSTRACT PUBMED 10631981

About this Structure

1C97 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

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

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