PDBsum entry 3og5

Protein binding

PDB id: 3og5

Contents

Protein chains

160 a.a. *

136 a.a. *

Waters ×50

* Residue conservation analysis

PDB id:

3og5

Name:

Protein binding

Title:

Crystal structure of bama potra45 tandem

Structure:

Outer membrane protein assembly complex, yaet protein. Chain: a, b. Fragment: potra45 domain (unp residues 264-424). Engineered: yes

Source:

Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: yaet. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.69Å R-factor: 0.216 R-free: 0.260

Authors:

P.Z.Gatzeva-Topalova,L.R.Warner,A.Pardi,M.C.Sousa

Key ref:

P.Z.Gatzeva-Topalova et al. (2010). Structure and flexibility of the complete periplasmic domain of BamA: the protein insertion machine of the outer membrane. Structure, 18, 1492-1501. PubMed id: 21070948

Date:

16-Aug-10 Release date: 17-Nov-10

Protein chain

P0A940  (BAMA_ECOLI) -  Outer membrane protein assembly factor BamA from Escherichia coli (strain K12)

Seq: 810 a.a.

Struc: 160 a.a.*

Protein chain

P0A940  (BAMA_ECOLI) -  Outer membrane protein assembly factor BamA from Escherichia coli (strain K12)

Seq: 810 a.a.

Struc: 136 a.a.

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Structure 18:1492-1501 (2010)

PubMed id: 21070948

Structure and flexibility of the complete periplasmic domain of BamA: the protein insertion machine of the outer membrane.

P.Z.Gatzeva-Topalova, L.R.Warner, A.Pardi, M.C.Sousa.

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.