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| | ==Crystal structure of the C-terminal domain of Escherichia coli lipoprotein BamC== | | ==Crystal structure of the C-terminal domain of Escherichia coli lipoprotein BamC== |
| - | <StructureSection load='3sns' size='340' side='right' caption='[[3sns]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='3sns' size='340' side='right'caption='[[3sns]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3sns]] is a 1 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=3SNS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SNS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3sns]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SNS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2laf|2laf]], [[2yh5|2yh5]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2laf|2laf]], [[2yh5|2yh5]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b2477, dapX, JW2462, nlpB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b2477, dapX, JW2462, nlpB ([https://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=3sns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sns OCA], [http://pdbe.org/3sns PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sns RCSB], [http://www.ebi.ac.uk/pdbsum/3sns PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sns ProSAT]</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=3sns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sns OCA], [https://pdbe.org/3sns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sns RCSB], [https://www.ebi.ac.uk/pdbsum/3sns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sns ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BAMC_ECOLI 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]<ref>PMID:20378773</ref> <ref>PMID:21823654</ref> <ref>PMID:22178970</ref> | + | [[https://www.uniprot.org/uniprot/BAMC_ECOLI 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]<ref>PMID:20378773</ref> <ref>PMID:21823654</ref> <ref>PMID:22178970</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/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Ecoli]] | | [[Category: Ecoli]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Aulakh, S]] | | [[Category: Aulakh, S]] |
| | [[Category: Kim, K H]] | | [[Category: Kim, K H]] |
| Structural highlights
Function
[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][1] [2] [3]
Publication Abstract from PubMed
In Gram-negative bacteria, the BAM complex catalyzes the essential process of assembling outer membrane proteins. The BAM complex in Escherichia coli consists of five proteins: one beta-barrel membrane protein, BamA, and four lipoproteins, BamB, BamC, BamD and BamE. Here, the crystal structure of the C-terminal domain of E. coli BamC (BamC(C): Ala224-Ser343) refined to 1.5 A resolution in space group H3 is reported. BamC(C) consists of a six-stranded antiparallel beta-sheet, three alpha-helices and one 3(10)-helix. Sequence and surface analysis reveals that most of the conserved residues within BamC(C) are localized to form a continuous negatively charged groove that is involved in a major crystalline lattice contact in which a helix from a neighbouring BamC(C) binds against this surface. This interaction is topologically and architecturally similar to those seen in the substrate-binding grooves of other proteins with BamC-like folds. Taken together, these results suggest that an identified surface on the C-terminal domain of BamC may serve as an important protein-binding surface for interaction with other BAM-complex components or substrates.
Crystallographic analysis of the C-terminal domain of the Escherichia coli lipoprotein BamC.,Kim KH, Aulakh S, Tan W, Paetzel M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt, 11):1350-8. Epub 2011 Oct 25. PMID:22102230[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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, Aulakh S, Tan W, Paetzel M. Crystallographic analysis of the C-terminal domain of the Escherichia coli lipoprotein BamC. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt, 11):1350-8. Epub 2011 Oct 25. PMID:22102230 doi:10.1107/S174430911103363X
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