4c00: Difference between revisions

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<StructureSection load='4c00' size='340' side='right'caption='[[4c00]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='4c00' size='340' side='right'caption='[[4c00]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4c00]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C00 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C00 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4c00]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C00 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MC3:1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE'>MC3</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MC3:1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE'>MC3</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bza|4bza]]</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=4c00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c00 OCA], [https://pdbe.org/4c00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c00 RCSB], [https://www.ebi.ac.uk/pdbsum/4c00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c00 ProSAT]</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=4c00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c00 OCA], [http://pdbe.org/4c00 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c00 RCSB], [http://www.ebi.ac.uk/pdbsum/4c00 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c00 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TAMA_ECOLI TAMA_ECOLI]] Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane. Has anion selective channel-forming ability, but the physiological relevance of this activity is unclear.<ref>PMID:22466966</ref> 
[[https://www.uniprot.org/uniprot/TAMA_ECOLI TAMA_ECOLI]] Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane. Has anion selective channel-forming ability, but the physiological relevance of this activity is unclear.<ref>PMID:22466966</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
TamA is an Escherichia coli Omp85 protein involved in autotransporter biogenesis. It comprises a 16-stranded transmembrane beta-barrel and three POTRA domains. The 2.3-A crystal structure reveals that the TamA barrel is closed at the extracellular face by a conserved lid loop. The C-terminal beta-strand of the barrel forms an unusual inward kink, which weakens the lateral barrel wall and creates a gate for substrate access to the lipid bilayer.
 
The structural basis of autotransporter translocation by TamA.,Gruss F, Zahringer F, Jakob RP, Burmann BM, Hiller S, Maier T Nat Struct Mol Biol. 2013 Sep 22. doi: 10.1038/nsmb.2689. PMID:24056943<ref>PMID:24056943</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4c00" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Burmann, B M]]
[[Category: Burmann BM]]
[[Category: Gruss, F]]
[[Category: Gruss F]]
[[Category: Hiller, S]]
[[Category: Hiller S]]
[[Category: Jakob, R P]]
[[Category: Jakob RP]]
[[Category: Maier, T]]
[[Category: Maier T]]
[[Category: Zaehringer, F]]
[[Category: Zaehringer F]]
[[Category: Autotransporter assembly]]
[[Category: Autotransporter biogenesis]]
[[Category: Outer membrane protein]]
[[Category: Polypeptide transport-associated]]
[[Category: Transport protein]]
[[Category: Ytfm]]
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