| Structural highlights
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
In Escherichia coli, the BAM complex catalyzes the essential process of assembling outer membrane proteins (OMPs). This complex consists of five proteins: one membrane-bound protein, BamA, and four lipoproteins, BamB, BamC, BamD, and BamE. Despite their importance in OMP biogenesis, there is currently a lack of functional and structural information on the BAM complex lipoproteins. BamE is the smallest but most conserved lipoprotein in the complex. The structural and dynamic properties of monomeric BamE (residues 21-133) were determined by NMR spectroscopy. The protein folds as two alpha-helices packed against a three-stranded antiparallel beta-sheet. The N-terminal (Ser21-Thr39) and C-terminal (Pro108-Asn113) residues, as well as a beta-hairpin loop (Val76-Gln89), are highly flexible on the subnanosecond time scale. BamE expressed and purified from E. coli also exists in a kinetically trapped dimeric state that has dramatically different NMR spectra, and hence structural features, relative to its monomeric form. The functional significance of the BamE dimer remains to be established. Structural comparison to proteins with a similar architecture suggests that BamE may play a role in mediating the association of the BAM complex or with the BAM complex substrates.
Structural Characterization of Escherichia coli BamE, a Lipoprotein Component of the beta-Barrel Assembly Machinery Complex.,Kim KH, Kang HS, Okon M, Escobar-Cabrera E, McIntosh LP, Paetzel M Biochemistry. 2011 Feb 15;50(6):1081-90. Epub 2011 Jan 24. PMID:21207987[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ 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
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