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2lae

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<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://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://www.rcsb.org/pdb/explore.do?structureId=2lae RCSB], [http://www.ebi.ac.uk/pdbsum/2lae PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/NLPB_ECOLI NLPB_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.<ref>PMID:20378773</ref> <ref>PMID:21823654</ref> <ref>PMID:22178970</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 19:06, 25 December 2014

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

Drag the structure with the mouse to rotate

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