2hh7: Difference between revisions

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[[Image:2hh7.gif|left|200px]]
{{Seed}}
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{{STRUCTURE_2hh7|  PDB=2hh7  |  SCENE=  }}  
{{STRUCTURE_2hh7|  PDB=2hh7  |  SCENE=  }}  


'''Crystal Structure of Cu(I) bound CsoR from Mycobacterium tuberculosis.'''
===Crystal Structure of Cu(I) bound CsoR from Mycobacterium tuberculosis.===




==Overview==
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Copper is an essential element that becomes highly cytotoxic when concentrations exceed the capacity of cells to sequester the ion. Here, we identify a new copper-specific repressor (CsoR) of a copper-sensitive operon (cso) in Mycobacterium tuberculosis (Mtb) that is representative of a large, previously uncharacterized family of proteins (DUF156). Electronic and X-ray absorption spectroscopies reveal that CsoR binds a single-monomer mole equivalent of Cu(I) to form a trigonally coordinated (S(2)N) Cu(I) complex. The 2.6-A crystal structure of copper-loaded CsoR shows a homodimeric antiparallel four-helix bundle architecture that represents a novel DNA-binding fold. The Cu(I) is coordinated by Cys36, Cys65' and His61' in a subunit bridging site. Cu(I) binding negatively regulates the binding of CsoR to a DNA fragment encompassing the operator-promoter region of the Mtb cso operon; this results in derepression of the operon in Mtb and the heterologous host Mycobacterium smegmatis. Substitution of Cys36 or His61 with alanine abolishes Cu(I)- and CsoR-dependent regulation in vivo and in vitro. Potential roles of CsoR in Mtb pathogenesis are discussed.
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==About this Structure==
==About this Structure==
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[[Category: Sacchettini,J C.]]
[[Category: Sacchettini,J C.]]
[[Category: 4-helix bundle]]
[[Category: 4-helix bundle]]
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