1u2w

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(New page: 200px<br /><applet load="1u2w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u2w, resolution 1.90&Aring;" /> '''Crystal Structure of...)
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[[Image:1u2w.gif|left|200px]]<br /><applet load="1u2w" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1u2w.gif|left|200px]]<br /><applet load="1u2w" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1u2w, resolution 1.90&Aring;" />
caption="1u2w, resolution 1.90&Aring;" />
'''Crystal Structure of the Staphylococcus aureus pI258 CadC'''<br />
'''Crystal Structure of the Staphylococcus aureus pI258 CadC'''<br />
==Overview==
==Overview==
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The Staphylococcus aureus plasmid pI258 cadCA operon encodes a P-type, ATPase, CadA, that confers resistance to the heavy metals Cd(II), Zn(II), and Pb(II). Expression of this heavy-metal efflux pump is regulated by, CadC, a homodimeric repressor that dissociates from the cad, operator/promoter upon binding of Cd(II), Pb(II), or Zn(II). CadC is a, member of the ArsR/SmtB family of metalloregulatory proteins. Here we, report the X-ray crystal structure of CadC at 1.9 angstroms resolution., The dimensions of the protein dimer are approximately 30 angstroms by 40, angstroms by 70 angstroms. Each monomer contains six alpha-helices and a, three-stranded beta-sheet. Helices 4 and 5 form a classic helix-turn-helix, motif that is the putative DNA binding region. The alpha1 helix of one, monomer crosses the dimer to approach the alpha4 helix of the other, monomer, consistent with the previous proposal that these two regulatory, metal binding sites for the inducer cadmium or lead are each formed by, Cys-7 and Cys-11 from the N terminus of one monomer and Cys-58 and Cys-60, of the other monomer. Two nonregulatory metal binding sites containing, zinc are formed between the two antiparallel alpha6 helices at the, dimerization interface. This is the first reported three-dimensional, structure of a member of the ArsR/SmtB family with regulatory metal, binding sites at the DNA binding domain and the first structure of a, transcription repressor that responds to the heavy metals Cd(II) and, Pb(II).
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The Staphylococcus aureus plasmid pI258 cadCA operon encodes a P-type ATPase, CadA, that confers resistance to the heavy metals Cd(II), Zn(II), and Pb(II). Expression of this heavy-metal efflux pump is regulated by CadC, a homodimeric repressor that dissociates from the cad operator/promoter upon binding of Cd(II), Pb(II), or Zn(II). CadC is a member of the ArsR/SmtB family of metalloregulatory proteins. Here we report the X-ray crystal structure of CadC at 1.9 angstroms resolution. The dimensions of the protein dimer are approximately 30 angstroms by 40 angstroms by 70 angstroms. Each monomer contains six alpha-helices and a three-stranded beta-sheet. Helices 4 and 5 form a classic helix-turn-helix motif that is the putative DNA binding region. The alpha1 helix of one monomer crosses the dimer to approach the alpha4 helix of the other monomer, consistent with the previous proposal that these two regulatory metal binding sites for the inducer cadmium or lead are each formed by Cys-7 and Cys-11 from the N terminus of one monomer and Cys-58 and Cys-60 of the other monomer. Two nonregulatory metal binding sites containing zinc are formed between the two antiparallel alpha6 helices at the dimerization interface. This is the first reported three-dimensional structure of a member of the ArsR/SmtB family with regulatory metal binding sites at the DNA binding domain and the first structure of a transcription repressor that responds to the heavy metals Cd(II) and Pb(II).
==About this Structure==
==About this Structure==
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1U2W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U2W OCA].
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1U2W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2W OCA].
==Reference==
==Reference==
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[[Category: Kandegedara, A.]]
[[Category: Kandegedara, A.]]
[[Category: Martin, P.]]
[[Category: Martin, P.]]
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[[Category: Rosen, B.P.]]
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[[Category: Rosen, B P.]]
[[Category: Ye, J.]]
[[Category: Ye, J.]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:48:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:02 2008''

Revision as of 13:20, 21 February 2008


1u2w, resolution 1.90Å

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Crystal Structure of the Staphylococcus aureus pI258 CadC

Overview

The Staphylococcus aureus plasmid pI258 cadCA operon encodes a P-type ATPase, CadA, that confers resistance to the heavy metals Cd(II), Zn(II), and Pb(II). Expression of this heavy-metal efflux pump is regulated by CadC, a homodimeric repressor that dissociates from the cad operator/promoter upon binding of Cd(II), Pb(II), or Zn(II). CadC is a member of the ArsR/SmtB family of metalloregulatory proteins. Here we report the X-ray crystal structure of CadC at 1.9 angstroms resolution. The dimensions of the protein dimer are approximately 30 angstroms by 40 angstroms by 70 angstroms. Each monomer contains six alpha-helices and a three-stranded beta-sheet. Helices 4 and 5 form a classic helix-turn-helix motif that is the putative DNA binding region. The alpha1 helix of one monomer crosses the dimer to approach the alpha4 helix of the other monomer, consistent with the previous proposal that these two regulatory metal binding sites for the inducer cadmium or lead are each formed by Cys-7 and Cys-11 from the N terminus of one monomer and Cys-58 and Cys-60 of the other monomer. Two nonregulatory metal binding sites containing zinc are formed between the two antiparallel alpha6 helices at the dimerization interface. This is the first reported three-dimensional structure of a member of the ArsR/SmtB family with regulatory metal binding sites at the DNA binding domain and the first structure of a transcription repressor that responds to the heavy metals Cd(II) and Pb(II).

About this Structure

1U2W is a Single protein structure of sequence from Staphylococcus aureus with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the Staphylococcus aureus pI258 CadC Cd(II)/Pb(II)/Zn(II)-responsive repressor., Ye J, Kandegedara A, Martin P, Rosen BP, J Bacteriol. 2005 Jun;187(12):4214-21. PMID:15937183

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