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==== | ==6-Deoxyerythronolide B synthase (DEBS) hybrid module (M3/1) in complex with antibody fragment 1B2== | ||
<StructureSection load='7m7e' size='340' side='right'caption='[[7m7e]]' scene=''> | <StructureSection load='7m7e' size='340' side='right'caption='[[7m7e]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7m7e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7M7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M7E FirstGlance]. <br> | ||
</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=7m7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m7e OCA], [https://pdbe.org/7m7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m7e RCSB], [https://www.ebi.ac.uk/pdbsum/7m7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m7e ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2Å</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=7m7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m7e OCA], [https://pdbe.org/7m7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m7e RCSB], [https://www.ebi.ac.uk/pdbsum/7m7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m7e ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/ERYA2_SACER ERYA2_SACER] [https://www.uniprot.org/uniprot/ERYA3_SACER ERYA3_SACER] [https://www.uniprot.org/uniprot/ERYA1_SACER ERYA1_SACER] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Assembly-line polyketide synthases, such as the 6-deoxyerythronolide B synthase (DEBS), are large enzyme factories prized for their ability to produce specific and complex polyketide products. By channeling protein-tethered substrates across multiple active sites in a defined linear sequence, these enzymes facilitate programmed small-molecule syntheses that could theoretically be harnessed to access countless polyketide product structures. Using cryogenic electron microscopy to study DEBS module 1, we present a structural model describing this substrate-channeling phenomenon. Our 3.2- to 4.3-angstrom-resolution structures of the intact module reveal key domain-domain interfaces and highlight an unexpected module asymmetry. We also present the structure of a product-bound module that shines light on a recently described "turnstile" mechanism for transient gating of active sites along the assembly line. | |||
Mapping the catalytic conformations of an assembly-line polyketide synthase module.,Cogan DP, Zhang K, Li X, Li S, Pintilie GD, Roh SH, Craik CS, Chiu W, Khosla C Science. 2021 Nov 5;374(6568):729-734. doi: 10.1126/science.abi8358. Epub 2021 , Nov 4. PMID:34735239<ref>PMID:34735239</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7m7e" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
*[[6-deoxyerythronolide B synthase 3D structures|6-deoxyerythronolide B synthase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharopolyspora erythraea]] | ||
[[Category: Chiu W]] | |||
[[Category: Cogan DP]] | |||
[[Category: Khosla C]] | |||
[[Category: Zhang K]] | |||
Latest revision as of 14:34, 30 October 2024
6-Deoxyerythronolide B synthase (DEBS) hybrid module (M3/1) in complex with antibody fragment 1B26-Deoxyerythronolide B synthase (DEBS) hybrid module (M3/1) in complex with antibody fragment 1B2
Structural highlights
FunctionERYA2_SACER ERYA3_SACER ERYA1_SACER Publication Abstract from PubMedAssembly-line polyketide synthases, such as the 6-deoxyerythronolide B synthase (DEBS), are large enzyme factories prized for their ability to produce specific and complex polyketide products. By channeling protein-tethered substrates across multiple active sites in a defined linear sequence, these enzymes facilitate programmed small-molecule syntheses that could theoretically be harnessed to access countless polyketide product structures. Using cryogenic electron microscopy to study DEBS module 1, we present a structural model describing this substrate-channeling phenomenon. Our 3.2- to 4.3-angstrom-resolution structures of the intact module reveal key domain-domain interfaces and highlight an unexpected module asymmetry. We also present the structure of a product-bound module that shines light on a recently described "turnstile" mechanism for transient gating of active sites along the assembly line. Mapping the catalytic conformations of an assembly-line polyketide synthase module.,Cogan DP, Zhang K, Li X, Li S, Pintilie GD, Roh SH, Craik CS, Chiu W, Khosla C Science. 2021 Nov 5;374(6568):729-734. doi: 10.1126/science.abi8358. Epub 2021 , Nov 4. PMID:34735239[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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