2n5d: Difference between revisions
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==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> | ||
<div class="pdbe-citations 2n5d" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Annaval, T]] | |||
[[Category: Chagot, B]] | |||
[[Category: Collin, S]] | |||
[[Category: Dorival, J]] | [[Category: Dorival, J]] | ||
[[Category: Gruez, A]] | [[Category: Gruez, A]] | ||
[[Category: Jacob, C]] | |||
[[Category: Risser, F]] | |||
[[Category: Roblin, P]] | [[Category: Roblin, P]] | ||
[[Category: | [[Category: Weissman, K J]] | ||
[[Category: | [[Category: Docking domain]] | ||
[[Category: | [[Category: Polyketide synthase]] | ||
[[Category: | [[Category: Protein binding]] | ||
Revision as of 04:58, 11 May 2016
NMR structure of PKS domains
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