3el6
From Proteopedia
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<StructureSection load='3el6' size='340' side='right'caption='[[3el6]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='3el6' size='340' side='right'caption='[[3el6]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3el6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3el6]] is a 1 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=3EL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EL6 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]] 1.85Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3el6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3el6 OCA], [https://pdbe.org/3el6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3el6 RCSB], [https://www.ebi.ac.uk/pdbsum/3el6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3el6 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=3el6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3el6 OCA], [https://pdbe.org/3el6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3el6 RCSB], [https://www.ebi.ac.uk/pdbsum/3el6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3el6 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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</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=3el6 ConSurf]. | </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=3el6 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The dehydratases (DHs) of modular polyketide synthases (PKSs) catalyze dehydrations that occur frequently in the biosynthesis of complex polyketides, yet little is known about them structurally or mechanistically. Here, the structure of a DH domain, isolated from the fourth module of the erythromycin PKS, is presented at 1.85 A resolution. As with the DH of the highly related animalian fatty acid synthase, the DH monomer possesses a double-hotdog fold. Two symmetry mates within the crystal lattice make a contact that likely represents the DH dimerization interface within an intact PKS. Conserved hydrophobic residues on the DH surface indicate potential interfaces with two other PKS domains, the ketoreductase and the acyl carrier protein. Mutation of an invariant arginine at the hypothesized acyl carrier protein docking site in the context of the erythromycin PKS resulted in decreased production of the erythromycin precursor 6-deoxyerythronolide B. The structure elucidates how the alpha-hydrogen and beta-hydroxyl group of a polyketide substrate interact with the catalytic histidine and aspartic acid in the DH active site prior to dehydration. | ||
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| - | Crystal structure of the erythromycin polyketide synthase dehydratase.,Keatinge-Clay A J Mol Biol. 2008 Dec 26;384(4):941-53. Epub 2008 Oct 11. PMID:18952099<ref>PMID:18952099</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3el6" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[6-deoxyerythronolide B synthase (DEBS)|6-deoxyerythronolide B synthase (DEBS)]] | *[[6-deoxyerythronolide B synthase (DEBS)|6-deoxyerythronolide B synthase (DEBS)]] | ||
*[[6-deoxyerythronolide B synthase 3D structures|6-deoxyerythronolide B synthase 3D structures]] | *[[6-deoxyerythronolide B synthase 3D structures|6-deoxyerythronolide B synthase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Saccharopolyspora erythraea]] |
| - | [[Category: | + | [[Category: Keatinge-Clay AT]] |
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Current revision
Crystal Structure of the Erythromycin Dehydratase
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