1ui6: Difference between revisions

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[[Image:1ui6.jpg|left|200px]]
{{Seed}}
[[Image:1ui6.png|left|200px]]


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{{STRUCTURE_1ui6|  PDB=1ui6  |  SCENE=  }}  
{{STRUCTURE_1ui6|  PDB=1ui6  |  SCENE=  }}  


'''Crystal structure of gamma-butyrolactone receptor (ArpA-like protein)'''
===Crystal structure of gamma-butyrolactone receptor (ArpA-like protein)===




==Overview==
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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.
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{{ABSTRACT_PUBMED_14757054}}


==About this Structure==
==About this Structure==
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[[Category: Alpha-helix bundle]]
[[Category: Alpha-helix bundle]]
[[Category: Helix-turn-helix]]
[[Category: Helix-turn-helix]]
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