2laf: Difference between revisions

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==NMR solution structure of the N-terminal domain of the E. coli lipoprotein BamC==
The line below this paragraph, containing "STRUCTURE_2laf", creates the "Structure Box" on the page.
<StructureSection load='2laf' size='340' side='right'caption='[[2laf]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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='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='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>
{{STRUCTURE_2laf|  PDB=2laf  |  SCENE=  }}
</table>
== Function ==
[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>  


===Solution structure of an E. coli lipoprotein===
==See Also==
 
*[[Bam complex 3D structures|Bam complex 3D structures]]
 
== References ==
==About this Structure==
<references/>
[[2laf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LAF OCA].
__TOC__
[[Category: Escherichia coli]]
</StructureSection>
[[Category: Pardi, A.]]
[[Category: Escherichia coli K-12]]
[[Category: Warner, L.]]
[[Category: Large Structures]]
[[Category: Pardi A]]
[[Category: Warner L]]

Latest revision as of 09:54, 1 May 2024

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

Structural highlights

2laf is a 1 chain structure with sequence from Escherichia coli K-12. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
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]

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
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