2laf: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==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== | ||
<StructureSection load='2laf' size='340' side='right' caption='[[2laf]], [[NMR_Ensembles_of_Models | 9 NMR models]]' scene=''> | <StructureSection load='2laf' size='340' side='right'caption='[[2laf]], [[NMR_Ensembles_of_Models | 9 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2laf]] is a 1 chain structure with sequence from [ | <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> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lae|2lae]]</td></tr> | </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> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nlpB, dapX, b2477, JW2462 ([ | <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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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 == | ||
[[ | [[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 == | ||
| Line 21: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Bam complex|Bam complex]] | *[[Bam complex 3D structures|Bam complex 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 27: | Line 27: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ecoli]] | [[Category: Ecoli]] | ||
[[Category: Large Structures]] | |||
[[Category: Pardi, A]] | [[Category: Pardi, A]] | ||
[[Category: Warner, L]] | [[Category: Warner, L]] | ||
Revision as of 10:39, 14 April 2021
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
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 PubMedThe 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. See AlsoReferences
|
| ||||||||||||||||||