5efr: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 5efr is ON HOLD  until Paper Publication
+==Crystal Structure of a BamA-BamD fusion==
+<StructureSection load='5efr' size='340' side='right'caption='[[5efr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5efr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodothermus_marinus Rhodothermus marinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EFR FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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=5efr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5efr OCA], [https://pdbe.org/5efr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5efr RCSB], [https://www.ebi.ac.uk/pdbsum/5efr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5efr ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/G2SES0_RHOMG G2SES0_RHOMG] [https://www.uniprot.org/uniprot/G2SI47_RHOMG G2SI47_RHOMG]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The beta-barrel assembly machine (BAM) mediates folding and insertion of integral beta-barrel outer membrane proteins (OMPs) in Gram-negative bacteria. Of the five BAM subunits, only BamA and BamD are essential for cell viability. Here we present the crystal structure of a fusion between BamA POTRA4-5 and BamD from Rhodothermus marinus. The POTRA5 domain binds BamD between its tetratricopeptide repeats 3 and 4. The interface structural elements are conserved in the Escherichia coli proteins, which allowed structure validation by mutagenesis and disulfide crosslinking in E. coli. Furthermore, the interface is consistent with previously reported mutations that impair BamA-BamD binding. The structure serves as a linchpin to generate a BAM model where POTRA domains and BamD form an elongated periplasmic ring adjacent to the membrane with a central cavity approximately 30 x 60 A wide. We propose that nascent OMPs bind this periplasmic ring prior to insertion and folding by BAM.
-Authors: Bergal, H.T., Hopkins, A.H., Metzner, S.I., Sousa, M.C.
+The Structure of a BamA-BamD Fusion Illuminates the Architecture of the beta-Barrel Assembly Machine Core.,Bergal HT, Hopkins AH, Metzner SI, Sousa MC Structure. 2015 Dec 29. pii: S0969-2126(15)00508-0. doi:, 10.1016/j.str.2015.10.030. PMID:26749448<ref>PMID:26749448</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Hopkins, A.H]]
+<div class="pdbe-citations 5efr" style="background-color:#fffaf0;"></div>
-[[Category: Sousa, M.C]]
-[[Category: Metzner, S.I]]
+==See Also==
-[[Category: Bergal, H.T]]
+*[[Bam complex 3D structures|Bam complex 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Rhodothermus marinus]]
+[[Category: Bergal HT]]
+[[Category: Hopkins AH]]
+[[Category: Metzner SI]]
+[[Category: Sousa MC]]