4BZA

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

Summary for 4BZA

Entry DOI	10.2210/pdb4bza/pdb
Related	4C00
Descriptor	TRANSLOCATION AND ASSEMBLY MODULE TAMA, 1,2-ETHANEDIOL (3 entities in total)
Functional Keywords	transport protein, polypeptide transport-associated, autotransporter biogenesis, outer membrane protein
Biological source	ESCHERICHIA COLI
Cellular location	Cell outer membrane: P0ADE4
Total number of polymer chains	1
Total formula weight	29535.30
Authors	Jakob, R.P.,Gruss, F.,Zaehringer, F.,Burmann, B.M.,Hiller, S.,Maier, T. (deposition date: 2013-07-24, release date: 2013-09-25, Last modification date: 2024-05-08)
Primary citation	Gruss, F.,Zaehringer, F.,Jakob, R.P.,Burmann, B.M.,Hiller, S.,Maier, T. The Structural Basis of Autotransporter Translocation by Tama Nat.Struct.Mol.Biol., 20:1318-, 2013 Cited by PubMed Abstract: TamA is an Escherichia coli Omp85 protein involved in autotransporter biogenesis. It comprises a 16-stranded transmembrane β-barrel and three POTRA domains. The 2.3-Å crystal structure reveals that the TamA barrel is closed at the extracellular face by a conserved lid loop. The C-terminal β-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. PubMed: 24056943 DOI: 10.1038/NSMB.2689 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.839 Å)

Structure validation