| Gene References into Functions |
- Free-energy calculations of lateral gate opening revealed a significantly lower barrier to opening in the C-terminal kinked conformation; mutagenesis experiments confirm the relevance of C-terminal kinking to BamA structure and function. PMID: 30087180
- Studied how the Bam complex accelerates folding and insertion through the assembly of a slow-folding beta-barrel substrate, LptD. Results suggest a mechanism in which substrate recruitment by periplasmic BamD regulates extracellular loop interactions to activate BamA for folding and insertion. PMID: 29463713
- we studied the assembly of an essential beta-barrel substrate for the Bam complex, BamA. By mutating conserved residues in the beta-barrel domain of this protein, we generated three assembly-defective BamA substrates that stall early in the folding process in the periplasm. Two of the three defective substrates, which harbor mutations within beta-strands, fail to associate productively with the Bam complex PMID: 28223520
- Data show that LptD is folded around LptE, and both components interact with the two essential beta-barrel assembly machine (Bam) components, BamA and BamD. PMID: 27439868
- The authors show that electrostatic interactions between the two essential proteins BamA and BamD coordinate conformational changes upon binding of unfolded substrate that allow the assembly reaction to proceed. PMID: 28760846
- Study investigated BamA flexibility using molecular dynamics simulations of BamA embedded in a model Escherichia coli outer membrane, reported that POTRA-membrane interactions influence the set of observed conformations PMID: 27332128
- BamD and BamA mutations cause a marked decrease in the levels of multimeric proteins. PMID: 27161117
- BamA alone can repeatedly facilitate the folding of OMPs PMID: 26394056
- Data show that disulfide crosslinks prevented lateral opening and exit pore formation resulting in a loss of outer membrane proteins BamA function, which can be fully rescued by the reductant tris(2-carboxyethyl)phosphine. PMID: 24980798
- structural analysis of BamB bound to a periplasmic domain fragment of BamA, the central component of the beta-barrel assembly machine PMID: 25468906
- BamA has five polypeptide transport-associated domains in its N-terminus, all of which are essential for BamA protein function. PMID: 24376817
- study determined the crystal structure of the C-terminal transmembrane domain of BamA at 2.6 A resolution; findings suggest the dome over the barrel may play an important role in maintaining the efficiency of OMP biogenesis PMID: 24619089
- These results suggest that the periplasmic region of BamA is firmly attached to the beta-barrel and does not experience fast global motion around the angle between POTRA 2 and 3. PMID: 24530687
- Our direct coupling analysis of BamA implicates residues R661 and D740 in a functional interaction. We find that the substitutions R661G and D740G each confer OM permeability defects and destabilize the BamA b-barrel PMID: 23934888
- Pull-down and Western blotting assays indicate that BamB interacts directly with the POTRA 1-3 domain of BamA PMID: 22948914
- the conserved (641)RGF(643) residues of the BamA L6 loop are important for BamA folding and biogenesis PMID: 22753067
- results imply that BamA and BamD interact directly with outer membrane protein substrates PMID: 22331884
- Taken together, these findings suggest that BamE modulates the conformation of BamA, likely through its interactions with BamD. PMID: 22178970
- Conditions that increase the folding of BamA demonstrate the ability of the reconstituted complex to catalyze more than one round of substrate assembly. PMID: 21823654
- the crystal structure of BamA POTRA4-5 has been determined to 1.50 A resolution with an R factor of 14.7% and an Rfree of 18.9% PMID: 21795783
- The data suggest that SurA and BamA POTRA 1 domain function in concert to assist folding and assembly of most beta-barrel outer membrane proteins except for TolC. PMID: 20598079
- The authors demonstrate that (i) BamA is essential for biogenesis of the trimeric auotransporter adhesins YadA, (ii) BamA interacts directly with YadA, (iii) the C-terminal amino acid motif of YadA is important for the BamA-dependent assembly. PMID: 20815824
- the periplasmic chaperone SurA and subunits of the Bam (Omp85) complex catalyse the insertion and assembly of outer-membrane proteins PMID: 19815580
- YaeT may have a role in outer membrane protein assembly in E. coli PMID: 15951436
- YaeT acts as a general outer membrane proteins assembly factor. PMID: 16102012
- YaeT, through its interaction with other outer membrane lipoproteins, forms a functional complex to assemble Escherichia coli membrane protein. PMID: 16824102
- YaeT is composed of two distinct domains, an amino-terminal periplasmic and a carboxy-terminal membrane domain; the periplasmic domain proves to be essential for in vivo function of YaeT PMID: 16829683
- Here we show that an essential and highly conserved gene product, YaeT, is the surface molecule recognized by the majority (ca. 70%) of Stx phages via conserved tail spike proteins PMID: 17693515
- crystal structure of a periplasmic fragment of YaeT reveals the polypeptide transport-associated (POTRA) domain fold and suggests a model for how POTRA domains can bind different peptide sequences PMID: 17702946
- Data show that YaeT-YfgL interaction invloves the region encompassing L173, L175, and R176 of YfgL and it was found that altering residues D227 and D229 in another region of YfgL from E221 to D229 resulted in defective YaeT bindings. PMID: 18165306
- Characterization of mutants resistant to contact-dependent growth inhibition (CDI) allowed the authors to identify BamA (YaeT) as the outer membrane receptor for CDI and AcrB as a potential downstream target. PMID: 18761695
- 1H, 13C and 15N chemical shift assignments and secondary structure of the YaeT POTRA domain; a domain found in the Omp85 family of proteins which is critical for insertion and folding of outer membrane proteins in Gram-negative bacteria PMID: 19636842
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