1td9: Difference between revisions

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-[[Image:1td9.jpg|left|200px]]<br /><applet load="1td9" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1td9, resolution 2.75&Aring;" />
-'''Crystal Structure of a Phosphotransacetylase from Bacillus subtilis'''<br />
-==Overview==
+==Crystal Structure of a Phosphotransacetylase from Bacillus subtilis==
-Phosphotransacetylase (Pta) [EC 2.3.1.8] plays a major role in acetate, metabolism by catalyzing the reversible transfer of the acetyl group, between coenzyme A (CoA) and orthophosphate:, CH(3)COSCoA+HPO(4)(2-)&lt;--&gt;CH(3)COOPO(3)(2-) +CoASH. In this study, we, report the crystal structures of Pta from Bacillus subtilis at 2.75 A, resolution and its complex with acetyl phosphate, one of its substrates, at 2.85 A resolution. In addition, the Pta activity of the enzyme has been, assayed. The enzyme folds into an alpha/beta architecture with two domains, separated by a prominent cleft, very similar to two other known Pta, structures. The enzyme-acetyl phosphate complex structure reveals a few, potential substrate binding sites. Two of them are located in the middle, of the interdomain cleft: each one is surrounded by a region of strictly, and highly conserved residues. High structural similarities are found with, 4-hydroxythreonine-4-phosphate dehydrogenase (PdxA), and isocitrate and, isopropylmalate dehydrogenases, all of which utilize NADP+ as their, cofactor, which binds in the interdomain cleft. Their substrate binding, sites are close to the acetyl phosphate binding sites of Pta in the cleft, as well. These results suggest that the CoA is likely to bind to the, interdomain cleft of Pta in a similar way as NADP+ binds to the other, three enzymes.
+<StructureSection load='1td9' size='340' side='right'caption='[[1td9]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1td9]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TD9 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1td9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1td9 OCA], [https://pdbe.org/1td9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1td9 RCSB], [https://www.ebi.ac.uk/pdbsum/1td9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1td9 ProSAT], [https://www.topsan.org/Proteins/BSGC/1td9 TOPSAN]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PTAS_BACSU PTAS_BACSU]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/td/1td9_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1td9 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Phosphotransacetylase (Pta) [EC 2.3.1.8] plays a major role in acetate metabolism by catalyzing the reversible transfer of the acetyl group between coenzyme A (CoA) and orthophosphate: CH(3)COSCoA+HPO(4)(2-)&lt;--&gt;CH(3)COOPO(3)(2-) +CoASH. In this study, we report the crystal structures of Pta from Bacillus subtilis at 2.75 A resolution and its complex with acetyl phosphate, one of its substrates, at 2.85 A resolution. In addition, the Pta activity of the enzyme has been assayed. The enzyme folds into an alpha/beta architecture with two domains separated by a prominent cleft, very similar to two other known Pta structures. The enzyme-acetyl phosphate complex structure reveals a few potential substrate binding sites. Two of them are located in the middle of the interdomain cleft: each one is surrounded by a region of strictly and highly conserved residues. High structural similarities are found with 4-hydroxythreonine-4-phosphate dehydrogenase (PdxA), and isocitrate and isopropylmalate dehydrogenases, all of which utilize NADP+ as their cofactor, which binds in the interdomain cleft. Their substrate binding sites are close to the acetyl phosphate binding sites of Pta in the cleft as well. These results suggest that the CoA is likely to bind to the interdomain cleft of Pta in a similar way as NADP+ binds to the other three enzymes.
-==About this Structure==
+Crystal structures of a phosphotransacetylase from Bacillus subtilis and its complex with acetyl phosphate.,Xu QS, Jancarik J, Lou Y, Kuznetsova K, Yakunin AF, Yokota H, Adams P, Kim R, Kim SH J Struct Funct Genomics. 2005 Dec;6(4):269-79. Epub 2005 Nov 9. PMID:16283428<ref>PMID:16283428</ref>
-TD9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TD9 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Crystal structures of a phosphotransacetylase from Bacillus subtilis and its complex with acetyl phosphate., Xu QS, Jancarik J, Lou Y, Kuznetsova K, Yakunin AF, Yokota H, Adams P, Kim R, Kim SH, J Struct Funct Genomics. 2005 Dec;6(4):269-79. Epub 2005 Nov 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16283428 16283428]
+</div>
+<div class="pdbe-citations 1td9" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Bacillus subtilis]]
-[[Category: Phosphate acetyltransferase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Jancarik J]]
-[[Category: BSGC, Berkeley.Structural.Genomics.Center.]]
+[[Category: Kim R]]
-[[Category: Jancarik, J.]]
+[[Category: Kim S-H]]
-[[Category: Kim, R.]]
+[[Category: Xu QS]]
-[[Category: Kim, S.H.]]
+[[Category: Yokota H]]
-[[Category: Xu, Q.S.]]
-[[Category: Yokota, H.]]
-[[Category: SO4]]
-[[Category: berkeley structural genomics center]]
-[[Category: bsgc structure funded by nih]]
-[[Category: protein structure initiative]]
-[[Category: psi]]
-[[Category: structural genomics]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:10:19 2007''