2alj
From Proteopedia
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Structure of the cis confomer of the major extracytoplasmic domain of the bacterial cell division protein divib from geobacillus stearothermophilus
Overview
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.
About this Structure
2ALJ is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
Domain architecture and structure of the bacterial cell division protein DivIB., Robson SA, King GF, Proc Natl Acad Sci U S A. 2006 Apr 25;103(17):6700-5. Epub 2006 Apr 17. PMID:16618922
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