4bza

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of TamA POTRA domains 1-3 from E. coli

Structural highlights

4bza is a 1 chain structure with sequence from Escherichia coli BL21(DE3). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.839Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Selkrig J, Mosbahi K, Webb CT, Belousoff MJ, Perry AJ, Wells TJ, Morris F, Leyton DL, Totsika M, Phan MD, Celik N, Kelly M, Oates C, Hartland EL, Robins-Browne RM, Ramarathinam SH, Purcell AW, Schembri MA, Strugnell RA, Henderson IR, Walker D, Lithgow T. Discovery of an archetypal protein transport system in bacterial outer membranes. Nat Struct Mol Biol. 2012 Apr 1;19(5):506-10, S1. doi: 10.1038/nsmb.2261. PMID:22466966 doi:10.1038/nsmb.2261
↑ Gruss F, Zahringer F, Jakob RP, Burmann BM, Hiller S, Maier T. The structural basis of autotransporter translocation by TamA. Nat Struct Mol Biol. 2013 Sep 22. doi: 10.1038/nsmb.2689. PMID:24056943 doi:10.1038/nsmb.2689

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4bza"

@@ Line 4: / Line 4: @@
 == 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='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>
+</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>
+[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 4bza" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4bza

From Proteopedia

Current revision

Crystal structure of TamA POTRA domains 1-3 from E. coli

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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