6fsu: Difference between revisions
New page: '''Unreleased structure''' The entry 6fsu is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Crystal structure of E.coli BamA beta-barrel with a C-terminal extension== | |||
<StructureSection load='6fsu' size='340' side='right' caption='[[6fsu]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6fsu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FSU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FSU 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=6fsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fsu OCA], [http://pdbe.org/6fsu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fsu RCSB], [http://www.ebi.ac.uk/pdbsum/6fsu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fsu ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/BAMA_ECO57 BAMA_ECO57]] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery.[HAMAP-Rule:MF_01430] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
beta-barrel outer membrane proteins (Omps) are key functional components of the outer membranes of Gram-negative bacteria, mitochondria, and plastids. In bacteria, their biogenesis requires the beta-barrel-assembly machinery (Bam) with the central insertase BamA, but the exact translocation and insertion mechanism remains elusive. The BamA insertase features a loosely closed gating region between the first and last beta-strand 16. Here, we describe approximately 70% complete sequence-specific NMR resonance assignments of the transmembrane region of the BamA beta-barrel in detergent micelles. On the basis of the assignments, NMR spectra show that the BamA barrel populates a conformational ensemble in slow exchange equilibrium, both in detergent micelles and lipid bilayer nanodiscs. Individual conformers can be selected from the ensemble by the introduction of a C-terminal strand extension, single-point mutations, or specific disulfide cross-linkings, and these modifications at the barrel seam are found to be allosterically coupled to sites at the entire barrel circumference. The resonance assignment provides a platform for mechanistic studies of BamA at atomic resolution, as well as for investigating interactions with potential antibiotic drugs and partner proteins. | |||
Sequence-Specific Solution NMR Assignments of the beta-Barrel Insertase BamA to Monitor Its Conformational Ensemble at the Atomic Level.,Hartmann JB, Zahn M, Burmann IM, Bibow S, Hiller S J Am Chem Soc. 2018 Sep 12;140(36):11252-11260. doi: 10.1021/jacs.8b03220. Epub, 2018 Sep 4. PMID:30125090<ref>PMID:30125090</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6fsu" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hartmann, J B]] | |||
[[Category: Hiller, S]] | |||
[[Category: Zahn, M]] | |||
[[Category: Membrane protein]] | |||
Latest revision as of 11:19, 14 November 2018
Crystal structure of E.coli BamA beta-barrel with a C-terminal extensionCrystal structure of E.coli BamA beta-barrel with a C-terminal extension
Structural highlights
Function[BAMA_ECO57] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery.[HAMAP-Rule:MF_01430] Publication Abstract from PubMedbeta-barrel outer membrane proteins (Omps) are key functional components of the outer membranes of Gram-negative bacteria, mitochondria, and plastids. In bacteria, their biogenesis requires the beta-barrel-assembly machinery (Bam) with the central insertase BamA, but the exact translocation and insertion mechanism remains elusive. The BamA insertase features a loosely closed gating region between the first and last beta-strand 16. Here, we describe approximately 70% complete sequence-specific NMR resonance assignments of the transmembrane region of the BamA beta-barrel in detergent micelles. On the basis of the assignments, NMR spectra show that the BamA barrel populates a conformational ensemble in slow exchange equilibrium, both in detergent micelles and lipid bilayer nanodiscs. Individual conformers can be selected from the ensemble by the introduction of a C-terminal strand extension, single-point mutations, or specific disulfide cross-linkings, and these modifications at the barrel seam are found to be allosterically coupled to sites at the entire barrel circumference. The resonance assignment provides a platform for mechanistic studies of BamA at atomic resolution, as well as for investigating interactions with potential antibiotic drugs and partner proteins. Sequence-Specific Solution NMR Assignments of the beta-Barrel Insertase BamA to Monitor Its Conformational Ensemble at the Atomic Level.,Hartmann JB, Zahn M, Burmann IM, Bibow S, Hiller S J Am Chem Soc. 2018 Sep 12;140(36):11252-11260. doi: 10.1021/jacs.8b03220. Epub, 2018 Sep 4. PMID:30125090[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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