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| | ==Structure of BamB fused to a BamA POTRA domain fragment== | | ==Structure of BamB fused to a BamA POTRA domain fragment== |
| - | <StructureSection load='4pk1' size='340' side='right' caption='[[4pk1]], [[Resolution|resolution]] 3.10Å' scene=''> | + | <StructureSection load='4pk1' size='340' side='right'caption='[[4pk1]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pk1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PK1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PK1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pk1]] 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=4PK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PK1 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=4pk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pk1 OCA], [http://pdbe.org/4pk1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pk1 RCSB], [http://www.ebi.ac.uk/pdbsum/4pk1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pk1 ProSAT]</span></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]] 3.1Å</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=4pk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pk1 OCA], [https://pdbe.org/4pk1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pk1 RCSB], [https://www.ebi.ac.uk/pdbsum/4pk1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pk1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BAMA_ECOLI 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.<ref>PMID:15951436</ref> <ref>PMID:16102012</ref> <ref>PMID:16824102</ref> <ref>PMID:20378773</ref> <ref>PMID:21823654</ref> | + | [https://www.uniprot.org/uniprot/BAMA_ECOLI 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.<ref>PMID:15951436</ref> <ref>PMID:16102012</ref> <ref>PMID:16824102</ref> <ref>PMID:20378773</ref> <ref>PMID:21823654</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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Bam complex|Bam complex]] | + | *[[Bam complex 3D structures|Bam complex 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Jansen, K B]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Sousa, M C]] | + | [[Category: Large Structures]] |
| - | [[Category: Bam complex]] | + | [[Category: Jansen KB]] |
| - | [[Category: Fusion]] | + | [[Category: Sousa MC]] |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4] [5] 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.[6] [7] [8] [9]
Publication Abstract from PubMed
The beta-Barrel Assembly Machinery (BAM) mediates folding and insertion of beta-barrel outer membrane proteins (OMPs) into the outer membrane of Gram-negative bacteria. BAM is a five protein complex consisting of the beta-barrel OMP BamA and lipoproteins BamB, C, D, and E. High resolution structures of all the individual BAM subunits and a BamD-BamC complex have been determined. However, the overall complex architecture remains elusive. BamA is the central component of BAM and consists of a membrane embedded beta-barrel and a periplasmic domain with five Polypeptide Translocation Associated (POTRA) motifs thought to interact with the accessory lipoproteins. Here we report the crystal structure of a fusion between BamB and a POTRA3-5 fragment of BamA. Extended loops 13 and 17 protruding from one end of the BamB beta-propeller contact the face of the POTRA3 beta-sheet in BamA. The interface is stabilized by several hydrophobic contacts, a network of hydrogen bonds, and a cation-pi interaction between BamA Y255 and BamB R195. Disruption of BamA:BamB binding by BamA Y255A and probing of the interface by disulfide bond crosslinking validate the physiological relevance of the observed interface. Furthermore, the structure is consistent with previously published mutagenesis studies. The periplasmic five-POTRA domain of BamA is flexible in solution due to hinge motions in the POTRA2-3 linker. Modeling BamB in complex with full-length BamA shows BamB binding at the POTRA2-3 hinge suggesting a role in modulation of BamA flexibility and the conformational changes associated with OMP folding and insertion.
Crystal Structure of BamB Bound to a Periplasmic Domain Fragment of BamA, the Central Component of the beta-Barrel Assembly Machine.,Jansen KB, Baker SL, Sousa MC J Biol Chem. 2014 Dec 2. pii: jbc.M114.584524. PMID:25468906[10]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ Noinaj N, Fairman JW, Buchanan SK. The Crystal Structure of BamB Suggests Interactions with BamA and Its Role within the BAM Complex. J Mol Biol. 2011 Jan 26. PMID:21277859 doi:10.1016/j.jmb.2011.01.042
- ↑ Jansen KB, Baker SL, Sousa MC. Crystal Structure of BamB Bound to a Periplasmic Domain Fragment of BamA, the Central Component of the beta-Barrel Assembly Machine. J Biol Chem. 2014 Dec 2. pii: jbc.M114.584524. PMID:25468906 doi:http://dx.doi.org/10.1074/jbc.M114.584524
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