2qo3: Difference between revisions
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<StructureSection load='2qo3' size='340' side='right'caption='[[2qo3]], [[Resolution|resolution]] 2.59Å' scene=''> | <StructureSection load='2qo3' size='340' side='right'caption='[[2qo3]], [[Resolution|resolution]] 2.59Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2qo3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2qo3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QO3 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.59Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CER:(2S,+3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE'>CER</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | |||
<tr id=' | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qo3 OCA], [https://pdbe.org/2qo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qo3 RCSB], [https://www.ebi.ac.uk/pdbsum/2qo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qo3 ProSAT]</span></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=2qo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qo3 OCA], [https://pdbe.org/2qo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qo3 RCSB], [https://www.ebi.ac.uk/pdbsum/2qo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qo3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/ERYA2_SACER ERYA2_SACER] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qo/2qo3_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qo/2qo3_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharopolyspora erythraea]] | ||
[[Category: | [[Category: Cane ED]] | ||
[[Category: | [[Category: Chen YA]] | ||
[[Category: | [[Category: Khosla C]] | ||
[[Category: | [[Category: Kim CY]] | ||
[[Category: | [[Category: Tang Y]] | ||
Latest revision as of 12:27, 6 November 2024
Crystal Structure of [KS3][AT3] didomain from module 3 of 6-deoxyerthronolide B synthaseCrystal Structure of [KS3][AT3] didomain from module 3 of 6-deoxyerthronolide B synthase
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe report the 2.6 A X-ray crystal structure of a 190 kDa homodimeric fragment from module 3 of the 6-deoxyerthronolide B synthase covalently bound to the inhibitor cerulenin. The structure shows two well-organized interdomain linker regions in addition to the full-length ketosynthase (KS) and acyltransferase (AT) domains. Analysis of the substrate-binding site of the KS domain suggests that a loop region at the homodimer interface influences KS substrate specificity. We also describe a model for the interaction of the catalytic domains with the acyl carrier protein (ACP) domain. The ACP is proposed to dock within a deep cleft between the KS and AT domains, with interactions that span both the KS homodimer and AT domain. In conjunction with other recent data, our results provide atomic resolution pictures of several catalytically relevant protein interactions in this remarkable family of modular megasynthases. Structural and mechanistic analysis of protein interactions in module 3 of the 6-deoxyerythronolide B synthase.,Tang Y, Chen AY, Kim CY, Cane DE, Khosla C Chem Biol. 2007 Aug;14(8):931-43. PMID:17719492[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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