6s3w
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Solution NMR Structure of TolAIII Bound to a Peptide Derived from the N-terminus of TolB== | |
+ | <StructureSection load='6s3w' size='340' side='right'caption='[[6s3w]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6s3w]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S3W 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=6s3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s3w OCA], [http://pdbe.org/6s3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s3w RCSB], [http://www.ebi.ac.uk/pdbsum/6s3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s3w ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Coordination of outer membrane constriction with septation is critical to faithful division in Gram-negative bacteria and vital to the barrier function of the membrane. This coordination requires the recruitment of the peptidoglycan-binding outer-membrane lipoprotein Pal at division sites by the Tol system. Here, we show that Pal accumulation at Escherichia coli division sites is a consequence of three key functions of the Tol system. First, Tol mobilises Pal molecules in dividing cells, which otherwise diffuse very slowly due to their binding of the cell wall. Second, Tol actively captures mobilised Pal molecules and deposits them at the division septum. Third, the active capture mechanism is analogous to that used by the inner membrane protein TonB to dislodge the plug domains of outer membrane TonB-dependent nutrient transporters. We conclude that outer membrane constriction is coordinated with cell division by active mobilisation-and-capture of Pal at division septa by the Tol system. | ||
- | + | The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism.,Szczepaniak J, Holmes P, Rajasekar K, Kaminska R, Samsudin F, Inns PG, Rassam P, Khalid S, Murray SM, Redfield C, Kleanthous C Nat Commun. 2020 Mar 11;11(1):1305. doi: 10.1038/s41467-020-15083-5. PMID:32161270<ref>PMID:32161270</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 6s3w" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Holmes, P]] | ||
+ | [[Category: Kleanthous, C]] | ||
+ | [[Category: Rajasekar, K]] | ||
+ | [[Category: Redfield, C]] | ||
+ | [[Category: Bacterial outer membrane]] | ||
+ | [[Category: Pal]] | ||
+ | [[Category: Protein binding]] | ||
+ | [[Category: Tola]] | ||
+ | [[Category: Tolb]] |
Revision as of 10:18, 27 March 2020
Solution NMR Structure of TolAIII Bound to a Peptide Derived from the N-terminus of TolB
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