2laf

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==NMR solution structure of the N-terminal domain of the E. coli lipoprotein BamC==
==NMR solution structure of the N-terminal domain of the E. coli lipoprotein BamC==
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<StructureSection load='2laf' size='340' side='right'caption='[[2laf]], [[NMR_Ensembles_of_Models | 9 NMR models]]' scene=''>
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<StructureSection load='2laf' size='340' side='right'caption='[[2laf]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2laf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LAF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2laf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LAF FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2lae|2lae]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nlpB, dapX, b2477, JW2462 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2laf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2laf OCA], [https://pdbe.org/2laf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2laf RCSB], [https://www.ebi.ac.uk/pdbsum/2laf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2laf 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=2laf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2laf OCA], [https://pdbe.org/2laf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2laf RCSB], [https://www.ebi.ac.uk/pdbsum/2laf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2laf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:21624375</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2laf" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Pardi, A]]
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[[Category: Pardi A]]
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[[Category: Warner, L]]
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[[Category: Warner L]]
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[[Category: Bam]]
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[[Category: Bamc]]
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[[Category: Beta-barrel assembly machinery]]
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[[Category: Membrane protein]]
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Current revision

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

PDB ID 2laf

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