3bkt
From Proteopedia
(New page: 200px<br /><applet load="3bkt" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bkt, resolution 1.500Å" /> '''Copper-bound C-term...) |
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- | [[Image:3bkt.jpg|left|200px]] | + | [[Image:3bkt.jpg|left|200px]] |
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- | '''Copper-bound C-terminal Domain of NikR''' | + | {{Structure |
+ | |PDB= 3bkt |SIZE=350|CAPTION= <scene name='initialview01'>3bkt</scene>, resolution 1.500Å | ||
+ | |SITE= <scene name='pdbsite=AC1:Cu+Binding+Site+For+Residue+C+1'>AC1</scene>, <scene name='pdbsite=AC2:Cu+Binding+Site+For+Residue+A+2'>AC2</scene>, <scene name='pdbsite=AC3:Cu+Binding+Site+For+Residue+D+3'>AC3</scene> and <scene name='pdbsite=AC4:Cu+Binding+Site+For+Residue+B+4'>AC4</scene> | ||
+ | |LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= nikR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
+ | }} | ||
+ | |||
+ | '''Copper-bound C-terminal Domain of NikR''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 3BKT is a [ | + | 3BKT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BKT OCA]. |
==Reference== | ==Reference== | ||
- | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18193897 18193897] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:59:49 2008'' |
Revision as of 16:59, 20 March 2008
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, resolution 1.500Å | |||||||
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Sites: | , , and | ||||||
Ligands: | |||||||
Gene: | nikR (Escherichia coli) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Copper-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.
About this Structure
3BKT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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