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TitleOuter membrane protein assembly mediated by BAM-SurA complexes.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 7612, Year 2024
Publish dateSep 1, 2024
AuthorsKatherine L Fenn / Jim E Horne / Joel A Crossley / Nils Böhringer / Romany J Horne / Till F Schäberle / Antonio N Calabrese / Sheena E Radford / Neil A Ranson /
PubMed AbstractThe outer membrane is a formidable barrier that protects Gram-negative bacteria against environmental threats. Its integrity requires the correct folding and insertion of outer membrane proteins ...The outer membrane is a formidable barrier that protects Gram-negative bacteria against environmental threats. Its integrity requires the correct folding and insertion of outer membrane proteins (OMPs) by the membrane-embedded β-barrel assembly machinery (BAM). Unfolded OMPs are delivered to BAM by the periplasmic chaperone SurA, but how SurA and BAM work together to ensure successful OMP delivery and folding remains unclear. Here, guided by AlphaFold2 models, we use disulphide bond engineering in an attempt to trap SurA in the act of OMP delivery to BAM, and solve cryoEM structures of a series of complexes. The results suggest that SurA binds BAM at its soluble POTRA-1 domain, which may trigger conformational changes in both BAM and SurA that enable transfer of the unfolded OMP to the BAM lateral gate for insertion into the outer membrane. Mutations that disrupt the interaction between BAM and SurA result in outer membrane assembly defects, supporting the key role of SurA in outer membrane biogenesis.
External linksNat Commun / PubMed:39218969 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 5.3 Å
Structure data

EMDB-18034, PDB-8pz1:
Wait Complex: Lateral open BAM bound Compact SurA
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-18035, PDB-8pz2:
Wait Complex: Lateral open BAM bound Extended SurA
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-18045, PDB-8pzu:
Wait Complex: BAM bound Darobactin-B and Compact SurA
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-18046, PDB-8pzv:
Wait Complex: BAM bound Darobactin-B and Extended SurA
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-18053, PDB-8q0g:
Release Complex: BAM bound EspP and Compact SurA
Method: EM (single particle) / Resolution: 4.3 Å

EMDB-18543, PDB-8qp5:
Release Complex: BAM bound EspP (SurA released)
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-18562, PDB-8qpu:
Release Complex: BAM bound EspP and Extended SurA
Method: EM (single particle) / Resolution: 5.2 Å

EMDB-18563, PDB-8qpv:
Handover Complex: BAM bound OmpX and extended SurA
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-18564, PDB-8qpw:
Arrival Complex: Lateral open BAM bound extended SurA plus OmpX
Method: EM (single particle) / Resolution: 5.3 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
  • photorhabdus heterorhabditis (bacteria)
KeywordsMEMBRANE PROTEIN / Outer Membrane / Complex / Chaperone / Protein Folding / Inhibitor

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