3og5: Difference between revisions

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<StructureSection load='3og5' size='340' side='right'caption='[[3og5]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
<StructureSection load='3og5' size='340' side='right'caption='[[3og5]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3og5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OG5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3og5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OG5 FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.69&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yaeT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=3og5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3og5 OCA], [https://pdbe.org/3og5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3og5 RCSB], [https://www.ebi.ac.uk/pdbsum/3og5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3og5 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=3og5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3og5 OCA], [https://pdbe.org/3og5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3og5 RCSB], [https://www.ebi.ac.uk/pdbsum/3og5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3og5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/D5CVA9_ECOKI D5CVA9_ECOKI]] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery (By similarity).[HAMAP-Rule:MF_01430]
[https://www.uniprot.org/uniprot/BAMA_ECOLI BAMA_ECOLI] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery.<ref>PMID:15951436</ref> <ref>PMID:16102012</ref> <ref>PMID:16824102</ref> <ref>PMID:20378773</ref> <ref>PMID:21823654</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Folding and insertion of beta-barrel outer membrane proteins (OMPs) is essential for Gram-negative bacteria. This process is mediated by the multiprotein complex BAM, composed of the essential beta-barrel OMP BamA and four lipoproteins (BamBCDE). The periplasmic domain of BamA is key for its function and contains five "polypeptide transport-associated" (POTRA) repeats. Here, we report the crystal structure of the POTRA4-5 tandem, containing the essential for BAM complex formation and cell viability POTRA5. The domain orientation observed in the crystal is validated by solution NMR and SAXS. Using previously determined structures of BamA POTRA1-4, we present a spliced model of the entire BamA periplasmic domain validated by SAXS. Solution scattering shows that conformational flexibility between POTRA2 and 3 gives rise to compact and extended conformations. The length of BamA in its extended conformation suggests that the protein may bridge the inner and outer membranes across the periplasmic space.
 
Structure and flexibility of the complete periplasmic domain of BamA: the protein insertion machine of the outer membrane.,Gatzeva-Topalova PZ, Warner LR, Pardi A, Sousa MC Structure. 2010 Nov 10;18(11):1492-501. PMID:21070948<ref>PMID:21070948</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3og5" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Gatzeva-Topalova, P Z]]
[[Category: Gatzeva-Topalova PZ]]
[[Category: Pardi, A]]
[[Category: Pardi A]]
[[Category: Sousa, M C]]
[[Category: Sousa MC]]
[[Category: Warner, L R]]
[[Category: Warner LR]]
[[Category: Insertion of outer membrane protein]]
[[Category: Potra fold]]
[[Category: Protein binding]]

Revision as of 11:16, 21 February 2024

Crystal Structure of BamA POTRA45 tandem

3og5, resolution 2.69Å

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