1aj8

From Proteopedia

Revision as of 12:44, 30 October 2007

CITRATE SYNTHASE FROM PYROCOCCUS FURIOSUS

Overview

The crystal structure of the closed form of citrate synthase, with citrate, and CoA bound, from the hyperthermophilic Archaeon Pyrococcus furiosus has, been determined to 1.9 A. This has allowed direct structural comparisons, between the same enzyme from organisms growing optimally at 37 degrees C, (pig), 55 degrees C (Thermoplasma acidophilum) and now 100 degrees C, (Pyrococcus furiosus). The three enzymes are homodimers and share a, similar overall fold, with the dimer interface comprising primarily an, eight alpha-helical sandwich of four antiparallel pairs of helices. The, active sites show similar modes of substrate binding; moreover, the, structural equivalence of the amino acid residues implicated in catalysis, implies that the mechanism proceeds via the same acid-base catalytic, ... [(full description)]

About this Structure

1AJ8 is a [Single protein] structure of sequence from [Pyrococcus furiosus] with COA and CIT as [ligands]. Active as [Transferred entry: 2.3.3.1], with EC number [4.1.3.7]. Structure known Active Sites: ACA and ACB. Full crystallographic information is available from [OCA].

Reference

The crystal structure of citrate synthase from the hyperthermophilic archaeon pyrococcus furiosus at 1.9 A resolution,., Russell RJ, Ferguson JM, Hough DW, Danson MJ, Taylor GL, Biochemistry. 1997 Aug 19;36(33):9983-94. PMID:9254593

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