1b0k
From Proteopedia
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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 , and as ligands. This structure supersedes 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
Page seeded by OCA on Thu Feb 21 11:50:13 2008
Categories: Aconitate hydratase | Single protein | Sus scrofa | Lauble, H. | Lloyd, S J. | Prasad, G S. | Stout, C D. | FLC | O | SF4 | Iron-sulfur | Lyase | Mitochondrion | Transit peptide | Tricarboxylic acid cycle
