1qo2: Difference between revisions

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OCA

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-[[Image:1qo2.gif|left|200px]]<br /><applet load="1qo2" size="450" color="white" frame="true" align="right" spinBox="true"
+==CRYSTAL STRUCTURE OF N-((5'-PHOSPHORIBOSYL)-FORMIMINO)-5-AMINOIMIDAZOL-4-CARBOXAMID RIBONUCLEOTID ISOMERASE (EC 3.1.3.15, HISA)==
-caption="1qo2, resolution 1.85&Aring;" />
+<StructureSection load='1qo2' size='340' side='right' caption='[[1qo2]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
-'''CRYSTAL STRUCTURE OF N-((5'-PHOSPHORIBOSYL)-FORMIMINO)-5-AMINOIMIDAZOL-4-CARBOXAMID RIBONUCLEOTID ISOMERASE (EC 3.1.3.15, HISA)'''<br />
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1qo2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QO2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QO2 FirstGlance]. <br>
+</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1thf|1thf]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">THISA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-lyxose_ketol-isomerase D-lyxose ketol-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.15 5.3.1.15] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qo2 OCA], [http://pdbe.org/1qo2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qo2 RCSB], [http://www.ebi.ac.uk/pdbsum/1qo2 PDBsum]</span></td></tr>
+</table>
+== 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/qo/1qo2_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/chain_selection.php?pdb_ID=2ata ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The atomic structures of two proteins in the histidine biosynthesis pathway consist of beta/alpha barrels with a twofold repeat pattern. It is likely that these proteins evolved by twofold gene duplication and gene fusion from a common half-barrel ancestor. These ancestral domains are not visible as independent domains in the extant proteins but can be inferred from a combination of sequence and structural analysis. The detection of subdomain structures may be useful in efforts to search genome sequences for functionally and structurally related proteins.
-==Overview==
+Structural evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion.,Lang D, Thoma R, Henn-Sax M, Sterner R, Wilmanns M Science. 2000 Sep 1;289(5484):1546-50. PMID:10968789<ref>PMID:10968789</ref>
-The atomic structures of two proteins in the histidine biosynthesis, pathway consist of beta/alpha barrels with a twofold repeat pattern. It is, likely that these proteins evolved by twofold gene duplication and gene, fusion from a common half-barrel ancestor. These ancestral domains are not, visible as independent domains in the extant proteins but can be inferred, from a combination of sequence and structural analysis. The detection of, subdomain structures may be useful in efforts to search genome sequences, for functionally and structurally related proteins.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-QO2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Active as [http://en.wikipedia.org/wiki/D-lyxose_ketol-isomerase D-lyxose ketol-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.15 5.3.1.15] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QO2 OCA].
+</div>
+<div class="pdbe-citations 1qo2" style="background-color:#fffaf0;"></div>
-==Reference==
+== References ==
-Structural evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion., Lang D, Thoma R, Henn-Sax M, Sterner R, Wilmanns M, Science. 2000 Sep 1;289(5484):1546-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10968789 10968789]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Atcc 43589]]
 [[Category: D-lyxose ketol-isomerase]]
-[[Category: Single protein]]
+[[Category: Lang, D]]
-[[Category: Thermotoga maritima]]
+[[Category: Sterner, R]]
-[[Category: Lang, D.]]
+[[Category: Thoma, R]]
-[[Category: Sterner, R.]]
+[[Category: Wilmanns, M]]
-[[Category: Thoma, R.]]
+[[Category: Histidine biosynthesis]]
-[[Category: Wilmanns, M.]]
+[[Category: Isomerase]]
-[[Category: histidine biosynthesis]]
+[[Category: Thermophilic protein]]
-[[Category: isomerase]]
-[[Category: thermophilic protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:50:29 2007''