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==Crystal structure of BamB and BamA P3-5 complex from E.coli== | ==Crystal structure of BamB and BamA P3-5 complex from E.coli== | ||
<StructureSection load='4xga' size='340' side='right' caption='[[4xga]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='4xga' size='340' side='right' caption='[[4xga]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
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== Function == | == Function == | ||
[[http://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> [[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> | [[http://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> [[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> | ||
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== Publication Abstract from PubMed == | |||
In Escherichia coli, the Omp85 protein BamA and four lipoproteins (BamBCDE) constitute the BAM complex, which is essential for the assembly and insertion of outer membrane proteins into the outer membrane. Here, the crystal structure of BamB in complex with the POTRA3-4 domains of BamA is reported at 2.1 A resolution. Based on this structure, the POTRA3 domain is associated with BamB via hydrogen-bonding and hydrophobic interactions. Structural and biochemical analysis revealed that the conserved residues Arg77, Glu127, Glu150, Ser167, Leu192, Leu194 and Arg195 of BamB play an essential role in interaction with the POTRA3 domain. | |||
Structural basis for the interaction of BamB with the POTRA3-4 domains of BamA.,Chen Z, Zhan LH, Hou HF, Gao ZQ, Xu JH, Dong C, Dong YH Acta Crystallogr D Struct Biol. 2016 Feb;72(Pt 2):236-44. doi:, 10.1107/S2059798315024729. Epub 2016 Jan 22. PMID:26894671<ref>PMID:26894671</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | == References == | ||
<references/> | <references/> | ||