3OG5

Crystal Structure of BamA POTRA45 tandem

Summary for 3OG5

• Entry DOI: 10.2210/pdb3og5/pdb
• Descriptor: Outer membrane protein assembly complex, YaeT protein (2 entities in total)
• Functional Keywords: potra fold, insertion of outer membrane proteins, protein binding
• Biological source: Escherichia coli
• Cellular location: Cell outer membrane (By similarity): D5CVA9
• Total number of polymer chains: 2
• Total formula weight: 37872.96

Authors

Gatzeva-Topalova, P.Z.,Warner, L.R.,Pardi, A.,Sousa, M.C. (deposition date: 2010-08-16, release date: 2010-11-17, Last modification date: 2024-10-16)

Primary citation

Gatzeva-Topalova, P.Z.,Warner, L.R.,Pardi, A.,Sousa, M.C.
Structure and Flexibility of the Complete Periplasmic Domain of BamA: The Protein Insertion Machine of the Outer Membrane
Structure, 18:1492-1501, 2010

PubMed Abstract: Folding and insertion of β-barrel outer membrane proteins (OMPs) is essential for Gram-negative bacteria. This process is mediated by the multiprotein complex BAM, composed of the essential β-barrel OMP BamA and four lipoproteins (BamBCDE). The periplasmic domain of BamA is key for its function and contains five "polypeptide transport-associated" (POTRA) repeats. Here, we report the crystal structure of the POTRA4-5 tandem, containing the essential for BAM complex formation and cell viability POTRA5. The domain orientation observed in the crystal is validated by solution NMR and SAXS. Using previously determined structures of BamA POTRA1-4, we present a spliced model of the entire BamA periplasmic domain validated by SAXS. Solution scattering shows that conformational flexibility between POTRA2 and 3 gives rise to compact and extended conformations. The length of BamA in its extended conformation suggests that the protein may bridge the inner and outer membranes across the periplasmic space.

PubMed: 21070948
DOI: 10.1016/j.str.2010.08.012

Experimental method

X-RAY DIFFRACTION (2.69 Å)