1qzt

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Revision as of 23:01, 20 November 2007

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spinqualitylabelsall models 1qzt, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Phosphotransacetylase from Methanosarcina thermophila

Overview

Phosphotransacetylase (Pta) [EC 2.3.1.8] is ubiquitous in the carbon, assimilation and energy-yielding pathways in anaerobic prokaryotes where, it catalyzes the reversible transfer of the acetyl group from acetyl, phosphate to CoA forming acetyl CoA and inorganic phosphate. The crystal, structure of Pta from the methane-producing archaeon Methanosarcina, thermophila, representing the first crystal structure of any Pta, was, determined by multiwavelength anomalous diffraction at 2.7 A resolution., In solution and in the crystal, the enzyme forms a homodimer. Each monomer, consists of two alpha/beta domains with a cleft along the domain boundary, which presumably contains the substrate binding sites. Comparison of the, four monomers present in the asymmetric unit indicates substantial, variations in the relative orientation of the two domains and the, structure of the putative active site cleft. A search for structural, homologs revealed the NADP(+)-dependent isocitrate and isopropylmalate, dehydrogenases as the only homologs with a similar two-domain, architecture.

About this Structure

1QZT is a Single protein structure of sequence from Methanosarcina thermophila with SO4 as ligand. Active as Phosphate acetyltransferase, with EC number 2.3.1.8 Full crystallographic information is available from OCA.

Reference

Crystal structure of phosphotransacetylase from the methanogenic archaeon Methanosarcina thermophila., Iyer PP, Lawrence SH, Luther KB, Rajashankar KR, Yennawar HP, Ferry JG, Schindelin H, Structure. 2004 Apr;12(4):559-67. PMID:15062079

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