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{{STRUCTURE_4bza|  PDB=4bza  |  SCENE=  }}
===Crystal structure of TamA POTRA domains 1-3 from E. coli===
{{ABSTRACT_PUBMED_24056943}}


==Function==
==Crystal structure of TamA POTRA domains 1-3 from E. coli==
[[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>
<StructureSection load='4bza' size='340' side='right'caption='[[4bza]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bza]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BZA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.839&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=4bza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bza OCA], [https://pdbe.org/4bza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bza RCSB], [https://www.ebi.ac.uk/pdbsum/4bza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bza ProSAT]</span></td></tr>
</table>
== Function ==
[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.


==About this Structure==
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>
[[4bza]] is a 1 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=4BZA OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<ref group="xtra">PMID:024056943</ref><references group="xtra"/><references/>
</div>
[[Category: Ecobd]]
<div class="pdbe-citations 4bza" style="background-color:#fffaf0;"></div>
[[Category: Burmann, B M.]]
== References ==
[[Category: Gruss, F.]]
<references/>
[[Category: Hiller, S.]]
__TOC__
[[Category: Jakob, R P.]]
</StructureSection>
[[Category: Maier, T.]]
[[Category: Large Structures]]
[[Category: Zaehringer, F.]]
[[Category: Burmann BM]]
[[Category: Autotransporter biogenesis]]
[[Category: Gruss F]]
[[Category: Outer membrane protein]]
[[Category: Hiller S]]
[[Category: Polypeptide transport-associated]]
[[Category: Jakob RP]]
[[Category: Transport protein]]
[[Category: Maier T]]
[[Category: Zaehringer F]]
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