1qzt
From Proteopedia
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'''Phosphotransacetylase from Methanosarcina thermophila''' | '''Phosphotransacetylase from Methanosarcina thermophila''' | ||
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[[Category: Schindelin, H.]] | [[Category: Schindelin, H.]] | ||
[[Category: Yennawar, H P.]] | [[Category: Yennawar, H P.]] | ||
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| - | [[Category: | + | [[Category: Acetyl phosphate]] |
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Revision as of 03:54, 3 May 2008
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. 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 Sat May 3 06:54:12 2008
