1YR1

Structure of the major extracytoplasmic domain of the trans isomer of the bacterial cell division protein divib from geobacillus stearothermophilus

Summary for 1YR1

• Entry DOI: 10.2210/pdb1yr1/pdb
• NMR Information: BMRB: 6395
• Descriptor: cell-division initiation protein (1 entity in total)
• Functional Keywords: cell-division initiation protein, divib, ftsq, divisome, cell cycle
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 1
• Total formula weight: 13365.08

Authors

Robson, S.A.,King, G.F. (deposition date: 2005-02-02, release date: 2006-02-07, Last modification date: 2024-05-01)

Primary citation

Robson, S.A.,King, G.F.
Domain architecture and structure of the bacterial cell division protein DivIB.
Proc.Natl.Acad.Sci.USA, 103:6700-6705, 2006

PubMed Abstract: Bacterial cytokinesis requires the coordinated assembly of a complex of proteins, collectively known as the divisome, at the incipient division site. DivIB/FtsQ is a conserved component of the divisome in bacteria with cell walls, suggesting that it plays a role in synthesis and/or remodeling of septal peptidoglycan. We demonstrate that the extracytoplasmic region of DivIB comprises three discrete domains that we designate alpha, beta, and gamma from the N to C terminus. The alpha-domain is proximal to the cytoplasmic membrane and coincident with the polypeptide transport-associated domain that was proposed previously to function as a molecular chaperone. The beta-domain has a unique 3D fold, with no eukaryotic counterpart, and we show that it interconverts between two discrete conformations via cis-trans isomerization of a Tyr-Pro peptide bond. We propose that this isomerization might modulate protein-protein interactions of the flanking alpha- and gamma-domains. The C-terminal gamma-domain is unstructured in the absence of other divisomal proteins, but we show that it is critical for DivIB function.

PubMed: 16618922
DOI: 10.1073/pnas.0601397103

Experimental method

SOLUTION NMR