2n5d

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m (Protected "2n5d" [edit=sysop:move=sysop])
Current revision (10:19, 15 March 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 2n5d is ON HOLD
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==NMR structure of PKS domains==
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<StructureSection load='2n5d' size='340' side='right'caption='[[2n5d]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2n5d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_virginiae Streptomyces virginiae]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2N5D FirstGlance]. <br>
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</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=2n5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n5d OCA], [https://pdbe.org/2n5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n5d RCSB], [https://www.ebi.ac.uk/pdbsum/2n5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n5d ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A4PHN0_STRVG A4PHN0_STRVG]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Dorival, J., Annaval, T., Risser, F., Collin, S., Roblin, P., Jacob, C., Gruez, A., Chagot, B., Weissman, K.J.
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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>
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Description: NMR structure of PKS domains
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Dorival, J]]
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<div class="pdbe-citations 2n5d" style="background-color:#fffaf0;"></div>
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[[Category: Collin, S]]
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== References ==
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[[Category: Gruez, A]]
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<references/>
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[[Category: Roblin, P]]
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__TOC__
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[[Category: Chagot, B]]
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</StructureSection>
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[[Category: Risser, F]]
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[[Category: Large Structures]]
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[[Category: Weissman, K.J]]
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[[Category: Streptomyces virginiae]]
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[[Category: Jacob, C]]
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[[Category: Annaval T]]
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[[Category: Annaval, T]]
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[[Category: Chagot B]]
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[[Category: Collin S]]
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[[Category: Dorival J]]
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[[Category: Gruez A]]
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[[Category: Jacob C]]
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[[Category: Risser F]]
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[[Category: Roblin P]]
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[[Category: Weissman KJ]]

Current revision

NMR structure of PKS domains

PDB ID 2n5d

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