|
|
| (3 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==Crystal Structure of BamA POTRA45 tandem== | | ==Crystal Structure of BamA POTRA45 tandem== |
| - | <StructureSection load='3og5' size='340' side='right' caption='[[3og5]], [[Resolution|resolution]] 2.69Å' scene=''> | + | <StructureSection load='3og5' size='340' side='right'caption='[[3og5]], [[Resolution|resolution]] 2.69Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3og5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OG5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OG5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3og5]] is a 2 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=3OG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OG5 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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]] 2.69Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yaeT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3og5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3og5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3og5 RCSB], [http://www.ebi.ac.uk/pdbsum/3og5 PDBsum]</span></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=3og5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3og5 OCA], [https://pdbe.org/3og5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3og5 RCSB], [https://www.ebi.ac.uk/pdbsum/3og5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3og5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/D5CVA9_ECOKI D5CVA9_ECOKI]] 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 (By similarity).[HAMAP-Rule:MF_01430] | + | [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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 17: |
Line 18: |
| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3og5" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Bam complex 3D structures|Bam complex 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Escherichia coli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Gatzeva-Topalova, P Z]]
| + | [[Category: Large Structures]] |
| - | [[Category: Pardi, A]] | + | [[Category: Gatzeva-Topalova PZ]] |
| - | [[Category: Sousa, M C]] | + | [[Category: Pardi A]] |
| - | [[Category: Warner, L R]] | + | [[Category: Sousa MC]] |
| - | [[Category: Insertion of outer membrane protein]] | + | [[Category: Warner LR]] |
| - | [[Category: Potra fold]] | + | |
| - | [[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]
Publication Abstract from PubMed
Folding and insertion of beta-barrel outer membrane proteins (OMPs) is essential for Gram-negative bacteria. This process is mediated by the multiprotein complex BAM, composed of the essential beta-barrel OMP BamA and four lipoproteins (BamBCDE). The periplasmic domain of BamA is key for its function and contains five "polypeptide transport-associated" (POTRA) repeats. Here, we report the crystal structure of the POTRA4-5 tandem, containing the essential for BAM complex formation and cell viability POTRA5. The domain orientation observed in the crystal is validated by solution NMR and SAXS. Using previously determined structures of BamA POTRA1-4, we present a spliced model of the entire BamA periplasmic domain validated by SAXS. Solution scattering shows that conformational flexibility between POTRA2 and 3 gives rise to compact and extended conformations. The length of BamA in its extended conformation suggests that the protein may bridge the inner and outer membranes across the periplasmic space.
Structure and flexibility of the complete periplasmic domain of BamA: the protein insertion machine of the outer membrane.,Gatzeva-Topalova PZ, Warner LR, Pardi A, Sousa MC Structure. 2010 Nov 10;18(11):1492-501. PMID:21070948[6]
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
- ↑ Gatzeva-Topalova PZ, Warner LR, Pardi A, Sousa MC. Structure and flexibility of the complete periplasmic domain of BamA: the protein insertion machine of the outer membrane. Structure. 2010 Nov 10;18(11):1492-501. PMID:21070948 doi:10.1016/j.str.2010.08.012
|
