PDBsum entry 5efr

Cell adhesion

PDB id: 5efr

Contents

Protein chain

403 a.a.

Waters ×208

PDB id:

5efr

Name:

Cell adhesion

Title:

Crystal structure of a bama-bamd fusion

Structure:

Bama-bamd fusion protein. Chain: a. Synonym: outer membrane protein assembly complex, yaet protein, outer membrane assembly lipoprotein yfio. Engineered: yes. Other_details: sequence mismatches to alanine are not mutations. They are unmodeled side chains.

Source:

Rhodothermus marinus. Organism_taxid: 29549. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.00Å R-factor: 0.212 R-free: 0.232

Authors:

H.T.Bergal,A.H.Hopkins,S.I.Metzner,M.C.Sousa

Key ref:

H.T.Bergal et al. (2016). The Structure of a BamA-BamD Fusion Illuminates the Architecture of the β-Barrel Assembly Machine Core. Structure, 24, 243-251. PubMed id: 26749448 DOI: 10.1016/j.str.2015.10.030

Date:

24-Oct-15 Release date: 27-Jan-16

Protein chain

Q8N5Z0  (AADAT_HUMAN) -  Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial from Homo sapiens

Seq: 425 a.a.

Struc: 403 a.a.*

* PDB and UniProt seqs differ at 356 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.str.2015.10.030

Structure 24:243-251 (2016)

PubMed id: 26749448

The Structure of a BamA-BamD Fusion Illuminates the Architecture of the β-Barrel Assembly Machine Core.

H.T.Bergal, A.H.Hopkins, S.I.Metzner, M.C.Sousa.

ABSTRACT

The β-barrel assembly machine (BAM) mediates folding and insertion of integral β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria. Of the five BAM subunits, only BamA and BamD are essential for cell viability. Here we present the crystal structure of a fusion between BamA POTRA4-5 and BamD from Rhodothermus marinus. The POTRA5 domain binds BamD between its tetratricopeptide repeats 3 and 4. The interface structural elements are conserved in the Escherichia coli proteins, which allowed structure validation by mutagenesis and disulfide crosslinking in E. coli. Furthermore, the interface is consistent with previously reported mutations that impair BamA-BamD binding. The structure serves as a linchpin to generate a BAM model where POTRA domains and BamD form an elongated periplasmic ring adjacent to the membrane with a central cavity approximately 30 × 60 Å wide. We propose that nascent OMPs bind this periplasmic ring prior to insertion and folding by BAM.