2km7
From Proteopedia
(Difference between revisions)
| (10 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Solution Structure of BamE, a component of the outer membrane protein assembly machinery in Escherichia coli== | |
| + | <StructureSection load='2km7' size='340' side='right'caption='[[2km7]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2km7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KM7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KM7 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2km7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2km7 OCA], [https://pdbe.org/2km7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2km7 RCSB], [https://www.ebi.ac.uk/pdbsum/2km7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2km7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/BAME_ECOLI BAME_ECOLI] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. May modulate the conformation of BamA, likely through interactions with BamD.<ref>PMID:17404237</ref> <ref>PMID:20378773</ref> <ref>PMID:21823654</ref> <ref>PMID:22178970</ref> <ref>PMID:21207987</ref> <ref>PMID:21586578</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential beta-barrel assembly machine (Bam). Here, we report the native structure and mechanism of a core component of this complex, BamE, and show that it is exclusively monomeric in its native environment of the periplasm, but is able to adopt a distinct dimeric conformation in the cytoplasm. BamE is shown to bind specifically to phosphatidylglycerol, and comprehensive mutagenesis and interaction studies have mapped key determinants for complex binding, outer membrane integrity and cell viability, as well as revealing the role of BamE within the Bam complex. | ||
| - | + | Structure and function of BamE within the outer membrane and the beta-barrel assembly machine.,Knowles TJ, Browning DF, Jeeves M, Maderbocus R, Rajesh S, Sridhar P, Manoli E, Emery D, Sommer U, Spencer A, Leyton DL, Squire D, Chaudhuri RR, Viant MR, Cunningham AF, Henderson IR, Overduin M EMBO Rep. 2011 Feb 1;12(2):123-8. Epub 2011 Jan 7. PMID:21212804<ref>PMID:21212804</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2km7" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Bam complex 3D structures|Bam complex 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Henderson IR]] | ||
| + | [[Category: Knowles TJ]] | ||
| + | [[Category: Manoli E]] | ||
| + | [[Category: Overduin M]] | ||
| + | [[Category: Rajesh S]] | ||
| + | [[Category: Sridhar P]] | ||
Current revision
Solution Structure of BamE, a component of the outer membrane protein assembly machinery in Escherichia coli
| |||||||||||
