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6c9u
From Proteopedia
(Difference between revisions)
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<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=6c9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c9u OCA], [http://pdbe.org/6c9u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c9u RCSB], [http://www.ebi.ac.uk/pdbsum/6c9u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c9u ProSAT]</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=6c9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c9u OCA], [http://pdbe.org/6c9u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c9u RCSB], [http://www.ebi.ac.uk/pdbsum/6c9u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c9u ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Catalytic modules of assembly-line polyketide synthases (PKSs) have previously been observed in two very different conformations-an "extended" architecture and an "arch-shaped" architecture-although the catalytic relevance of neither has been directly established. By the use of a fully human naive antigen-binding fragment (Fab) library, a high-affinity antibody was identified that bound to the extended conformation of a PKS module, as verified by X-ray crystallography and tandem size-exclusion chromatography-small-angle X-ray scattering (SEC-SAXS). Kinetic analysis proved that this antibody-stabilized module conformation was fully competent for catalysis of intermodular polyketide chain translocation as well as intramodular polyketide chain elongation and functional group modification of a growing polyketide chain. Thus, the extended conformation of a PKS module is fully competent for all of its essential catalytic functions. | ||
| + | |||
| + | Structure-Function Analysis of the Extended Conformation of a Polyketide Synthase Module.,Li X, Sevillano N, La Greca F, Deis L, Liu YC, Deller MC, Mathews II, Matsui T, Cane DE, Craik CS, Khosla C J Am Chem Soc. 2018 May 18. doi: 10.1021/jacs.8b02100. PMID:29762030<ref>PMID:29762030</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6c9u" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 05:54, 30 May 2018
Crystal structure of [KS3][AT3] didomain from module 3 of 6-deoxyerthronolide B synthase in complex with antibody fragment (Fab)
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