1wae

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==Overview==
==Overview==
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Copper nitrite reductases contain both an electron-transfer type 1 Cu site, and a catalytic type 2 Cu site. We have mutated one of the type 2 copper, ligating histidines to observe the effect on catalytic turnover. This, mutation has created a unique site where Cu is ligated by 2 His Nepsilon2, atoms alone.
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Copper nitrite reductases contain both an electron-transfer type 1 Cu site and a catalytic type 2 Cu site. We have mutated one of the type 2 copper ligating histidines to observe the effect on catalytic turnover. This mutation has created a unique site where Cu is ligated by 2 His Nepsilon2 atoms alone.
==About this Structure==
==About this Structure==
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[[Category: Achromobacter xylosoxidans]]
[[Category: Achromobacter xylosoxidans]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Transferred entry: 1.7.2.1]]
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[[Category: Transferred entry: 1 7.2 1]]
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[[Category: Antonyuk, S.V.]]
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[[Category: Antonyuk, S V.]]
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[[Category: Eady, R.R.]]
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[[Category: Eady, R R.]]
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[[Category: Ellis, M.J.]]
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[[Category: Ellis, M J.]]
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[[Category: Hasnain, S.S.]]
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[[Category: Hasnain, S S.]]
[[Category: Sawers, G.]]
[[Category: Sawers, G.]]
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[[Category: Strange, R.W.]]
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[[Category: Strange, R W.]]
[[Category: CU]]
[[Category: CU]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: reductase]]
[[Category: reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:21:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:11 2008''

Revision as of 13:42, 21 February 2008


1wae, resolution 1.95Å

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CRYSTAL STRUCTURE OF H129V MUTANT OF ALCALIGENES XYLOSOXIDANS NITRITE REDUCTASE

Overview

Copper nitrite reductases contain both an electron-transfer type 1 Cu site and a catalytic type 2 Cu site. We have mutated one of the type 2 copper ligating histidines to observe the effect on catalytic turnover. This mutation has created a unique site where Cu is ligated by 2 His Nepsilon2 atoms alone.

About this Structure

1WAE is a Single protein structure of sequence from Achromobacter xylosoxidans with and as ligands. Active as Transferred entry: 1.7.2.1, with EC number 1.7.99.3 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Observation of an unprecedented Cu Bis-His site: crystal structure of the H129V mutant of nitrite reductase., Ellis MJ, Antonyuk SV, Strange RW, Sawers G, Eady RR, Hasnain SS, Inorg Chem. 2004 Nov 29;43(24):7591-3. PMID:15554622

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