2km7

From Proteopedia

(Difference between revisions)

Revision as of 04:34, 10 September 2015

Solution Structure of BamE, a component of the outer membrane protein assembly machinery in Escherichia coli

Structural highlights

2km7 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

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^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sklar JG, Wu T, Gronenberg LS, Malinverni JC, Kahne D, Silhavy TJ. Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli. Proc Natl Acad Sci U S A. 2007 Apr 10;104(15):6400-5. Epub 2007 Apr 2. PMID:17404237 doi:10.1073/pnas.0701579104
↑ Hagan CL, Kim S, Kahne D. Reconstitution of outer membrane protein assembly from purified components. Science. 2010 May 14;328(5980):890-2. doi: 10.1126/science.1188919. Epub 2010 Apr, 8. PMID:20378773 doi:10.1126/science.1188919
↑ Hagan CL, Kahne D. The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of beta-barrel assembly. Biochemistry. 2011 Sep 6;50(35):7444-6. doi: 10.1021/bi2010784. Epub 2011 Aug 11. PMID:21823654 doi:10.1021/bi2010784
↑ Rigel NW, Schwalm J, Ricci DP, Silhavy TJ. BamE modulates the Escherichia coli beta-barrel assembly machine component BamA. J Bacteriol. 2012 Mar;194(5):1002-8. doi: 10.1128/JB.06426-11. Epub 2011 Dec 16. PMID:22178970 doi:10.1128/JB.06426-11
↑ Kim KH, Kang HS, Okon M, Escobar-Cabrera E, McIntosh LP, Paetzel M. Structural Characterization of Escherichia coli BamE, a Lipoprotein Component of the beta-Barrel Assembly Machinery Complex. Biochemistry. 2011 Feb 15;50(6):1081-90. Epub 2011 Jan 24. PMID:21207987 doi:10.1021/bi101659u
↑ Albrecht R, Zeth K. Structural basis of outer membrane protein biogenesis in bacteria. J Biol Chem. 2011 Aug 5;286(31):27792-803. Epub 2011 May 17. PMID:21586578 doi:10.1074/jbc.M111.238931
↑ 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. Structure and function of BamE within the outer membrane and the beta-barrel assembly machine. EMBO Rep. 2011 Feb 1;12(2):123-8. Epub 2011 Jan 7. PMID:21212804 doi:10.1038/embor.2010.202

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2km7"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2km7]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KM7 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=2km7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2km7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2km7 RCSB], [http://www.ebi.ac.uk/pdbsum/2km7 PDBsum]</span></td></tr>
+</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=2km7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2km7 OCA], [http://pdbe.org/2km7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2km7 RCSB], [http://www.ebi.ac.uk/pdbsum/2km7 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 15: @@
 From MEDLINE&reg;/PubMed&reg;, 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|Bam complex]]
 == References ==
 <references/>

2km7

From Proteopedia

Revision as of 04:34, 10 September 2015

Solution Structure of BamE, a component of the outer membrane protein assembly machinery in Escherichia coli

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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