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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]] 2.15&Aring;' scene=''>
<StructureSection load='4xga' size='340' side='right'caption='[[4xga]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4xga]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XGA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XGA FirstGlance]. <br>
<table><tr><td colspan='2'>[[4xga]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XGA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XGA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=4xga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xga OCA], [http://pdbe.org/4xga PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xga RCSB], [http://www.ebi.ac.uk/pdbsum/4xga PDBsum]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bamB, yfgL, b2512, JW2496 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), bamA, yaeT, yzzN, yzzY, b0177, JW0172 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4xga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xga OCA], [http://pdbe.org/4xga PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xga RCSB], [http://www.ebi.ac.uk/pdbsum/4xga PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xga ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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</div>
</div>
<div class="pdbe-citations 4xga" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4xga" style="background-color:#fffaf0;"></div>
==See Also==
*[[Bam complex 3D structures|Bam complex 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Large Structures]]
[[Category: Chen, Z]]
[[Category: Chen, Z]]
[[Category: Dong, C]]
[[Category: Dong, C]]

Revision as of 10:33, 29 May 2019

Crystal structure of BamB and BamA P3-5 complex from E.coliCrystal structure of BamB and BamA P3-5 complex from E.coli

Structural highlights

4xga is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:bamB, yfgL, b2512, JW2496 (ECOLI), bamA, yaeT, yzzN, yzzY, b0177, JW0172 (ECOLI)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.[1] [2] [3] [4] [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.[5] [6] [7] [8] [9]

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[10]

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

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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
  7. ↑ 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
  8. ↑ 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
  9. ↑ 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
  10. ↑ Chen Z, Zhan LH, Hou HF, Gao ZQ, Xu JH, Dong C, Dong YH. Structural basis for the interaction of BamB with the POTRA3-4 domains of BamA. Acta Crystallogr D Struct Biol. 2016 Feb;72(Pt 2):236-44. doi:, 10.1107/S2059798315024729. Epub 2016 Jan 22. PMID:26894671 doi:http://dx.doi.org/10.1107/S2059798315024729

4xga, resolution 2.15Å

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