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2kt2

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'''Unreleased structure'''
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{{Seed}}
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[[Image:2kt2.jpg|left|200px]]
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The entry 2kt2 is ON HOLD until Paper Publication
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{{STRUCTURE_2kt2| PDB=2kt2 | SCENE= }}
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Authors: Ledwidge, R., Danacea, F., Dotsch, V., Miller, S.M.
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===Structure of NmerA, the N-terminal HMA domain of Tn501 Mercuric Reductase===
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Description: Structure of NmerA, the N-terminal HMA domain of Tn501 Mercuric Reductase
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 25 12:48:46 2010''
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{{ABSTRACT_PUBMED_20828160}}
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==About this Structure==
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2KT2 is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KT2 OCA].
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==Reference==
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<ref group="xtra">PMID:20828160</ref><ref group="xtra">PMID:16114877</ref><references group="xtra"/>
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Danacea, F.]]
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[[Category: Dotsch, V.]]
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[[Category: Ledwidge, R.]]
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[[Category: Miller, S M.]]
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[[Category: Hma domain]]
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[[Category: Mera]]
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[[Category: Mercuric reductase]]
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[[Category: Mercuric resistance]]
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[[Category: Metal-binding]]
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[[Category: Nmera]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 22 14:41:23 2010''

Revision as of 11:32, 22 September 2010

Template:STRUCTURE 2kt2

Structure of NmerA, the N-terminal HMA domain of Tn501 Mercuric Reductase

Template:ABSTRACT PUBMED 20828160

About this Structure

2KT2 is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full experimental information is available from OCA.

Reference

  • Ledwidge R, Hong B, Doetsch V, Miller SM. NmerA of Tn501 Mercuric Ion Reductase: Structural Modulation of the pKa Values of the Metal Binding Cysteine Thiols. Biochemistry. 2010 Sep 9. PMID:20828160 doi:10.1021/bi100537f
  • Ledwidge R, Patel B, Dong A, Fiedler D, Falkowski M, Zelikova J, Summers AO, Pai EF, Miller SM. NmerA, the metal binding domain of mercuric ion reductase, removes Hg2+ from proteins, delivers it to the catalytic core, and protects cells under glutathione-depleted conditions. Biochemistry. 2005 Aug 30;44(34):11402-16. PMID:16114877 doi:10.1021/bi050519d

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