1b0k

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Revision as of 09:08, 20 November 2007

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spinqualitylabelsall models 1b0k, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

S642A:FLUOROCITRATE COMPLEX OF ACONITASE

Overview

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 --> 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.

About this Structure

1B0K is a Single protein structure of sequence from Sus scrofa with FLC, SF4 and O as ligands. This structure superseeds the now removed PDB entry 1AS9. Active as Aconitate hydratase, with EC number 4.2.1.3 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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