1ui6
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1ui6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ui6, resolution 2.40Å" /> '''Crystal structure of...)
Next diff →
Revision as of 01:54, 25 November 2007
|
Crystal structure of gamma-butyrolactone receptor (ArpA-like protein)
Overview
The gamma-butyrolactone-type autoregulator/receptor systems in the, Gram-positive bacterial genus Streptomyces regulate morphological, differentiation or antibiotic production, or both. The autoregulator, receptors act as DNA-binding proteins, and on binding their cognate, ligands (gamma-butyrolactones) they are released from the DNA, thus, serving as repressors. The crystal structure of CprB in Streptomyces, coelicolor A3(2), a homologue of the A-factor-receptor protein, ArpA, in, Streptomyces griseus, was determined. The overall structure of CprB shows, that the gamma-butyrolactone receptors belong to the TetR family. CprB is, composed of two domains, a DNA-binding domain and a regulatory domain. The, regulatory domain contains a hydrophobic cavity, which probably serves as, a ligand-binding pocket. On the basis of the crystal structure of CprB and, on the analogy of the characteristics of ligand-TetR binding, the binding, of gamma-butyrolactones to the regulatory domain of the receptors is, supposed to induce the relocation of the DNA-binding domain through, conformational changes of residues located between the ligand-binding site, and the DNA-binding domain, which would result in the dissociation of the, receptors from their target DNA.
About this Structure
1UI6 is a Single protein structure of sequence from Streptomyces coelicolor. Full crystallographic information is available from OCA.
Reference
Crystal structure of a gamma-butyrolactone autoregulator receptor protein in Streptomyces coelicolor A3(2)., Natsume R, Ohnishi Y, Senda T, Horinouchi S, J Mol Biol. 2004 Feb 13;336(2):409-19. PMID:14757054
Page seeded by OCA on Sun Nov 25 04:02:31 2007
