2n5d
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==NMR structure of PKS domains== | |
| + | <StructureSection load='2n5d' size='340' side='right' caption='[[2n5d]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2n5d]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N5D FirstGlance]. <br> | ||
| + | </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=2n5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n5d OCA], [http://pdbe.org/2n5d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n5d RCSB], [http://www.ebi.ac.uk/pdbsum/2n5d PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Modular polyketide synthases (PKSs) direct the biosynthesis of clinically valuable secondary metabolites in bacteria. The fidelity of chain growth depends on specific recognition between successive subunits in each assembly line: interactions mediated by C- and N-terminal "docking domains" (DDs). We have identified a new family of DDs in trans-acyl transferase PKSs, exemplified by a matched pair from the virginiamycin (Vir) system. In the absence of C-terminal partner (VirA CDD) or a downstream catalytic domain, the N-terminal DD (VirFG NDD) exhibits multiple characteristics of an intrinsically disordered protein. Fusion of the two docking domains results in a stable fold for VirFG NDD and an overall protein-protein complex of unique topology whose structure we support by site-directed mutagenesis. Furthermore, using small-angle X-ray scattering (SAXS), the positions of the flanking acyl carrier protein and ketosynthase domains have been identified, allowing modeling of the complete intersubunit interface. | ||
| - | + | Characterization of Intersubunit Communication in the Virginiamycin trans-Acyl Transferase Polyketide Synthase.,Dorival J, Annaval T, Risser F, Collin S, Roblin P, Jacob C, Gruez A, Chagot B, Weissman KJ J Am Chem Soc. 2016 Mar 16. PMID:26982529<ref>PMID:26982529</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 2n5d" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Annaval, T]] | ||
| + | [[Category: Chagot, B]] | ||
[[Category: Collin, S]] | [[Category: Collin, S]] | ||
| + | [[Category: Dorival, J]] | ||
[[Category: Gruez, A]] | [[Category: Gruez, A]] | ||
| - | [[Category: Roblin, P]] | ||
| - | [[Category: Chagot, B]] | ||
| - | [[Category: Risser, F]] | ||
| - | [[Category: Weissman, K.J]] | ||
[[Category: Jacob, C]] | [[Category: Jacob, C]] | ||
| - | [[Category: | + | [[Category: Risser, F]] |
| + | [[Category: Roblin, P]] | ||
| + | [[Category: Weissman, K J]] | ||
| + | [[Category: Docking domain]] | ||
| + | [[Category: Polyketide synthase]] | ||
| + | [[Category: Protein binding]] | ||
Revision as of 04:58, 11 May 2016
NMR structure of PKS domains
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