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2lae

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Revision as of 19:26, 1 August 2018

NMR solution structure of the C-terminal domain of the E. coli lipoprotein BamC

Structural highlights

2lae is a 1 chain structure with sequence from Ecoli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2laf
Gene:	nlpB, dapX, b2477, JW2462 (ECOLI)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

The CS-RDC-NOE Rosetta program was used to generate the solution structure of a 27-kDa fragment of the Escherichia coli BamC protein from a limited set of NMR data. The BamC protein is a component of the essential five-protein beta-barrel assembly machine in E. coli. The first 100 residues in BamC were disordered in solution. The Rosetta calculations showed that BamC(101-344) forms two well-defined domains connected by an approximately 18-residue linker, where the relative orientation of the domains was not defined. Both domains adopt a helix-grip fold previously observed in the Bet v 1 superfamily. (15)N relaxation data indicated a high degree of conformational flexibility for the linker connecting the N-terminal domain and the C-terminal domain in BamC. The results here show that CS-RDC-NOE Rosetta is robust and has a high tolerance for misassigned nuclear Overhauser effect restraints, greatly simplifying NMR structure determinations.

Structure of the BamC Two-Domain Protein Obtained by Rosetta with a Limited NMR Data Set.,Warner LR, Varga K, Lange OF, Baker SL, Baker D, Sousa MC, Pardi A J Mol Biol. 2011 Aug 5;411(1):83-95. Epub 2011 May 23. PMID:21624375^[4]

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

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
↑ Warner LR, Varga K, Lange OF, Baker SL, Baker D, Sousa MC, Pardi A. Structure of the BamC Two-Domain Protein Obtained by Rosetta with a Limited NMR Data Set. J Mol Biol. 2011 Aug 5;411(1):83-95. Epub 2011 May 23. PMID:21624375 doi:10.1016/j.jmb.2011.05.022

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2lae"

@@ Line 6: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2laf|2laf]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nlpB, dapX, b2477, JW2462 ([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=2lae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lae OCA], [http://pdbe.org/2lae PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lae RCSB], [http://www.ebi.ac.uk/pdbsum/2lae PDBsum]</span></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=2lae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lae OCA], [http://pdbe.org/2lae PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lae RCSB], [http://www.ebi.ac.uk/pdbsum/2lae PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lae ProSAT]</span></td></tr>
 </table>
 == Function ==

2lae

From Proteopedia

Revision as of 19:26, 1 August 2018

NMR solution structure of the C-terminal domain of the E. coli lipoprotein BamC

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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