| Structural highlights
5d0q is a 8 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | NonStd Res: | |
| Related: | 5d0o |
| Gene: | bamA, yaeT, yzzN, yzzY, b0177, JW0172 ("Bacillus coli" Migula 1895), bamC, dapX, nlpB, b2477, JW2462 ("Bacillus coli" Migula 1895), bamD, yfiO, b2595, JW2577 ("Bacillus coli" Migula 1895), bamE, smpA, b2617, JW2598 ("Bacillus coli" Migula 1895) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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] [BAMA_ECOLI] 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.[7] [8] [9] [10] [11] [BAMD_ECOLI] 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 BamA, the core component of the assembly machinery. Probably involved in transient protein interactions.[HAMAP-Rule:MF_00922][12] [13] [14] [15] [16] [BAMC_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.[HAMAP-Rule:MF_00924][17] [18] [19]
Publication Abstract from PubMed
All Gram-negative bacteria, mitochondria and chloroplasts have outer membrane proteins (OMPs) that perform many fundamental biological processes. The OMPs in Gram-negative bacteria are inserted and folded into the outer membrane by the beta-barrel assembly machinery (BAM). The mechanism involved is poorly understood, owing to the absence of a structure of the entire BAM complex. Here we report two crystal structures of the Escherichia coli BAM complex in two distinct states: an inward-open state and a lateral-open state. Our structures reveal that the five polypeptide transport-associated domains of BamA form a ring architecture with four associated lipoproteins, BamB-BamE, in the periplasm. Our structural, functional studies and molecular dynamics simulations indicate that these subunits rotate with respect to the integral membrane beta-barrel of BamA to induce movement of the beta-strands of the barrel and promote insertion of the nascent OMP.
Structural basis of outer membrane protein insertion by the BAM complex.,Gu Y, Li H, Dong H, Zeng Y, Zhang Z, Paterson NG, Stansfeld PJ, Wang Z, Zhang Y, Wang W, Dong C Nature. 2016 Mar 3;531(7592):64-9. doi: 10.1038/nature17199. Epub 2016 Feb 22. PMID:26901871[20]
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
- ↑ Doerrler WT, Raetz CR. Loss of outer membrane proteins without inhibition of lipid export in an Escherichia coli YaeT mutant. J Biol Chem. 2005 Jul 29;280(30):27679-87. Epub 2005 Jun 10. PMID:15951436 doi:http://dx.doi.org/M504796200
- ↑ Werner J, Misra R. YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli. Mol Microbiol. 2005 Sep;57(5):1450-9. PMID:16102012 doi:http://dx.doi.org/MMI4775
- ↑ Malinverni JC, Werner J, Kim S, Sklar JG, Kahne D, Misra R, Silhavy TJ. YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli. Mol Microbiol. 2006 Jul;61(1):151-64. PMID:16824102 doi:http://dx.doi.org/10.1111/j.1365-2958.2006.05211.x
- ↑ 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
- ↑ Malinverni JC, Werner J, Kim S, Sklar JG, Kahne D, Misra R, Silhavy TJ. YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli. Mol Microbiol. 2006 Jul;61(1):151-64. PMID:16824102 doi:http://dx.doi.org/10.1111/j.1365-2958.2006.05211.x
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ Dong C, Hou HF, Yang X, Shen YQ, Dong YH. Structure of Escherichia coli BamD and its functional implications in outer membrane protein assembly. Acta Crystallogr D Biol Crystallogr. 2012 Feb;68(Pt 2):95-101. Epub 2012 Jan 6. PMID:22281737 doi:10.1107/S0907444911051031
- ↑ 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
- ↑ Gu Y, Li H, Dong H, Zeng Y, Zhang Z, Paterson NG, Stansfeld PJ, Wang Z, Zhang Y, Wang W, Dong C. Structural basis of outer membrane protein insertion by the BAM complex. Nature. 2016 Mar 3;531(7592):64-9. doi: 10.1038/nature17199. Epub 2016 Feb 22. PMID:26901871 doi:http://dx.doi.org/10.1038/nature17199
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