3bkf: Difference between revisions

Revision as of 20:13, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3bkf.png

Template:STRUCTURE 3bkf

Zinc-bound C-terminal Domain of NikRZinc-bound C-terminal Domain of NikR

Template:ABSTRACT PUBMED 18193897

About this StructureAbout this Structure

3BKF is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structural Basis of the Metal Specificity for Nickel Regulatory Protein NikR(,)., Phillips CM, Schreiter ER, Guo Y, Wang SC, Zamble DB, Drennan CL, Biochemistry. 2008 Feb 19;47(7):1938-46. Epub 2008 Jan 15. PMID:18193897

Page seeded by OCA on Mon Jul 28 20:13:15 2008

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OCA

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-'''Zinc-bound C-terminal Domain of NikR'''
+===Zinc-bound C-terminal Domain of NikR===
-==Overview==
+<!--
-In the presence of excess nickel, Escherichia coli NikR regulates cellular nickel uptake by suppressing the transcription of the nik operon, which encodes the nickel uptake transporter, NikABCDE. Previously published in vitro studies have shown that NikR is capable of binding a range of divalent transition metal ions in addition to Ni2+, including Co2+, Cu2+, Zn2+, and Cd2+. To understand how the high-affinity nickel binding site of NikR is able to accommodate these other metal ions, and to improve our understanding of NikR's mechanism of binding to DNA, we have determined structures of the metal-binding domain (MBD) of NikR in the apo form and in complex with Cu2+ and Zn2+ ions and compared them with the previously published structures with Ni2+. We observe that Cu2+ ions bind in a manner very similar to that of Ni2+, with a square planar geometry but with longer bond lengths. Crystals grown in the presence of Zn2+ reveal a protein structure similar to that of apo MBD with a disordered alpha3 helix, but with two electron density peaks near the Ni2+ binding site corresponding to two Zn2+ ions. These structural findings along with biochemical data on NikR support a hypothesis that ordering of the alpha3 helix is important for repressor activation.
+The line below this paragraph, {{ABSTRACT_PUBMED_18193897}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_18193897}}
 ==About this Structure==
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 [[Category: Transcription factor]]
 [[Category: Transcription regulation]]
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