3prw

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Crystal structure of the lipoprotein BamB

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Categories: Escherichia coli K-12 | Large Structures | Clausen T | Heuck A

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 <StructureSection load='3prw' size='340' side='right'caption='[[3prw]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3prw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PRW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PRW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3prw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PRW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PRW FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yfgL, b2512, JW2496 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#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=3prw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3prw OCA], [https://pdbe.org/3prw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3prw RCSB], [https://www.ebi.ac.uk/pdbsum/3prw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3prw ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/BAMB_ECOLI BAMB_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, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins.<ref>PMID:20378773</ref> <ref>PMID:21823654</ref> <ref>PMID:21586578</ref> <ref>PMID:21277859</ref>
+[https://www.uniprot.org/uniprot/BAMB_ECOLI BAMB_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, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins.<ref>PMID:20378773</ref> <ref>PMID:21823654</ref> <ref>PMID:21586578</ref> <ref>PMID:21277859</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-beta-Barrel proteins are frequently found in the outer membrane of mitochondria, chloroplasts and Gram-negative bacteria. In Escherichia coli, these proteins are inserted in the outer membrane by the Bam (beta-barrel assembly machinery) complex, a multiprotein machinery formed by the beta-barrel protein BamA and the four peripheral membrane proteins BamB, BamC, BamD and BamE. The periplasmic part of BamA binds prefolded beta-barrel proteins by a beta-augmentation mechanism, thereby stabilizing the precursors prior to their membrane insertion. However, the role of the associated proteins within the Bam complex remains unknown. Here, we describe the crystal structure of BamB, a nonessential component of the Bam complex. The structure shows a typical eight-bladed beta-propeller fold. Two sequence stretches of BamB were previously identified to be important for interaction with BamA. In our structure, both motifs are located in close proximity to each other and contribute to a conserved region forming a narrow groove on the top of the propeller. Moreover, crystal contacts reveal two interaction modes of how BamB might bind unfolded beta-barrel proteins. In the crystal lattice, BamB binds to exposed beta-strands by beta-augmentation, whereas peptide stretches rich in aromatic residues can be accommodated in hydrophobic pockets located at the bottom of the propeller. Thus, BamB could simultaneously bind to BamA and prefolded beta-barrel proteins, thereby enhancing the folding and membrane insertion capability of the Bam complex.
-Augmenting beta-augmentation: structural basis of how BamB binds BamA and may support folding of outer membrane proteins.,Heuck A, Schleiffer A, Clausen T J Mol Biol. 2011 Mar 11;406(5):659-66. Epub 2011 Jan 12. PMID:21236263<ref>PMID:21236263</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3prw" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 25: / Line 16: @@
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Clausen, T]]
+[[Category: Clausen T]]
-[[Category: Heuck, A]]
+[[Category: Heuck A]]
-[[Category: Beta propeller]]
-[[Category: Structural protein]]

3prw

From Proteopedia

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Crystal structure of the lipoprotein BamB

Structural highlights

Function

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