1qzt

<table><tr><td colspan='2'>[[1qzt]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_1825 Dsm 1825]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1QZT FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qzs|1qzs]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2210 DSM 1825])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphate_acetyltransferase Phosphate acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.8 2.3.1.8] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1qzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qzt OCA], [http://pdbe.org/1qzt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qzt RCSB], [http://www.ebi.ac.uk/pdbsum/1qzt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qzt ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15062079</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1qzt" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Dsm 1825]]

[[Category: Phosphate acetyltransferase]]

[[Category: Ferry, J G]]

[[Category: Iyer, P P]]

[[Category: Lawrence, S H]]

[[Category: Luther, K B]]

[[Category: Rajashankar, K R]]

[[Category: Schindelin, H]]

[[Category: Yennawar, H P]]

[[Category: Transferase]]