3Q6B: The High-Resolution And New Form Crystal Structure Of Bama Potra4-5 From E.Coli

In Escherichia coli, the BAM complex is employed to mediate correct folding of the outer membrane (OM) proteins into beta-barrels and their insertion into the OM. BamA, which is an essential component of the complex, consists of a C-terminal transmembrane region and five N-terminal polypeptide transport-associated (POTRA) domains. Although deletion studies have shown that each of the POTRA domains plays an important role in the process of BAM complex formation, only POTRA5 is essential for cell viability. Here, the crystal structure of POTRA4-5 has been determined to 1.50 A resolution with an R factor of 14.7% and an R(free) of 18.9%.
PDB ID: 3Q6BDownload
MMDB ID: 92529
PDB Deposition Date: 2010/12/31
Updated in MMDB: 2011/08
Experimental Method:
x-ray diffraction
Resolution: 1.5  Å
Source Organism:
Similar Structures:
Biological Unit for 3Q6B: monomeric; determined by author and by software (PISA)
Molecular Components in 3Q6B
Label Count Molecule
Protein (1 molecule)
Outer Membrane Protein Assembly Complex, Yaet Protein
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB