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1ui5
From Proteopedia
(New page: 200px<br /><applet load="1ui5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ui5, resolution 2.40Å" /> '''Crystal structure of...) |
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| - | [[Image:1ui5.jpg|left|200px]]<br /><applet load="1ui5" size=" | + | [[Image:1ui5.jpg|left|200px]]<br /><applet load="1ui5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ui5, resolution 2.40Å" /> | caption="1ui5, resolution 2.40Å" /> | ||
'''Crystal structure of gamma-butyrolactone receptor (ArpA like protein)'''<br /> | '''Crystal structure of gamma-butyrolactone receptor (ArpA like protein)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The gamma-butyrolactone-type autoregulator/receptor systems in the | + | 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== | ==About this Structure== | ||
| - | 1UI5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http:// | + | 1UI5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UI5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: helix-turn-helix]] | [[Category: helix-turn-helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:24:51 2008'' |
Revision as of 13:24, 21 February 2008
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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
1UI5 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
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