Center for Structural Genomics of Infectious Diseases

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Structure of IDP00456

CSGID target: IDP00456
PDB Id: 3GSD (NCBI MMDB)
Authors: 'G.Minasov,Z.Wawrzak,T.Skarina,O.Onopriyenko,S.N.Peterson,A.Savchenko,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid)'
Responsible person: George Minasov
Responsible lab: Northwestern University
Deposition Date: Mar 26, 2009
Release Date: Apr 07, 2009

Description: CutA are a protein family present in bacteria, plants, and animals, including humans. Escherichia coli CutA is involved in copper tolerance, whereas mammalian proteins are implicated in the anchoring of acetylcholinesterase in neuronal cell membranes. Here we report crystal structure of the divalent-cation tolerance protein CutA from Yersinia pestis. Biological assembly is a homo trimer. Each subunit consists of a ferredoxin-like (beta1alpha1beta2beta3alpha2beta4) fold with an additional strand (beta5), a C-terminal helix (alpha3), and an unusual extended beta-hairpin involving strands beta2 and beta3. The evolutionarily conserved trimeric assembly of CutA is reminiscent of the architecture of PII signal transduction proteins. This similarity suggests an intriguing role of CutA proteins in signal transduction through allosteric communications between subunits.
Functional assignment: Divalent-cation tolerance protein

Ligand code	Name	Ligand type
EPE		crystallization
NA		crystallization
PEG		crystallization
175	3,5-dihydro-5-methylidene-4h-imidazol-4-on