1qzt
From Proteopedia
|
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
Page seeded by OCA on Wed Nov 21 01:09:03 2007
Categories: Methanosarcina thermophila | Phosphate acetyltransferase | Single protein | Ferry, J.G. | Iyer, P.P. | Lawrence, S.H. | Luther, K.B. | Rajashankar, K.R. | Schindelin, H. | Yennawar, H.P. | SO4 | Acetate metabolism | Acetyl coenzyme a (acetyl coa) | Acetyl phosphate | Coenzyme a (coa) | Phosphotransacetylase (pta)
