1QZT

Phosphotransacetylase from Methanosarcina thermophila

Summary for 1QZT

• Entry DOI: 10.2210/pdb1qzt/pdb
• Related: 1QZS
• Descriptor: Phosphate acetyltransferase, SULFATE ION (3 entities in total)
• Functional Keywords: phosphotransacetylase (pta), coenzyme a (coa), acetyl coenzyme a (acetyl coa), acetyl phosphate, acetate metabolism, transferase
• Biological source: Methanosarcina thermophila
• Total number of polymer chains: 4
• Total formula weight: 142086.66

Authors

Iyer, P.P.,Lawrence, S.H.,Luther, K.B.,Rajashankar, K.R.,Yennawar, H.P.,Ferry, J.G.,Schindelin, H. (deposition date: 2003-09-17, release date: 2004-06-22, Last modification date: 2024-02-14)

Primary citation

Iyer, P.P.,Lawrence, S.H.,Luther, K.B.,Rajashankar, K.R.,Yennawar, H.P.,Ferry, J.G.,Schindelin, H.
Crystal structure of phosphotransacetylase from the methanogenic archaeon Methanosarcina thermophila.
STRUCTURE, 12:559-567, 2004

PubMed Abstract: 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.

PubMed: 15062079
DOI: 10.1016/j.str.2004.03.007

Experimental method

X-RAY DIFFRACTION (2.7 Å)