4bza

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

spinqualitylabelsall models 4bza, resolution 1.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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: EDO 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA