2yh6: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Structure of the N-terminal domain of BamC from E. coli== | ==Structure of the N-terminal domain of BamC from E. coli== | ||
<StructureSection load='2yh6' size='340' side='right' caption='[[2yh6]], [[Resolution|resolution]] 1.55Å' scene=''> | <StructureSection load='2yh6' size='340' side='right'caption='[[2yh6]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2yh6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecobd Ecobd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YH6 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[2yh6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecobd Ecobd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YH6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2YH6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yh5|2yh5]], [[2yh3|2yh3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yh5|2yh5]], [[2yh3|2yh3]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2yh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yh6 OCA], [http://pdbe.org/2yh6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yh6 RCSB], [http://www.ebi.ac.uk/pdbsum/2yh6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yh6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| 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: Ecobd]] | [[Category: Ecobd]] | ||
[[Category: Large Structures]] | |||
[[Category: Albrecht, R]] | [[Category: Albrecht, R]] | ||
[[Category: Zeth, K]] | [[Category: Zeth, K]] | ||
[[Category: Lipid binding protein]] | [[Category: Lipid binding protein]] | ||
Revision as of 15:51, 22 July 2020
Structure of the N-terminal domain of BamC from E. coliStructure of the N-terminal domain of BamC from E. coli
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 PubMedIn Escherichia coli, a multicomponent BAM (beta-barrel assembly machinery) complex is responsible for recognition and assembly of outer membrane beta-barrel proteins. The functionality of BAM in protein biogenesis is mainly orchestrated through the presence of two essential components, BamA and BamD. Here, we present crystal structures of four lipoproteins (BamB-E). Monomeric BamB and BamD proteins display scaffold architectures typically implied in transient protein interactions. BamB is a beta-propeller protein comprising eight WD40 repeats. BamD shows an elongated fold on the basis of five tetratricopeptide repeats, three of which form the scaffold for protein recognition. The rod-shaped BamC protein has evolved through the gene duplication of two conserved domains known to mediate protein interactions in structurally related complexes. By contrast, the dimeric BamE is formed through a domain swap and indicates fold similarity to the beta-lactamase inhibitor protein family, possibly integrating cell wall stability in BAM function. Structural and biochemical data show evidence for the specific recognition of amphipathic sequences through the tetratricopeptide repeat architecture of BamD. Collectively, our data advance the understanding of the BAM complex and highlight the functional importance of BamD in amphipathic outer membrane beta-barrel protein motif recognition and protein delivery. Structural basis of outer membrane protein biogenesis in bacteria.,Albrecht R, Zeth K J Biol Chem. 2011 Aug 5;286(31):27792-803. Epub 2011 May 17. PMID:21586578[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||