1oe1
From Proteopedia
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==Overview== | ==Overview== | ||
| - | We provide the first atomic resolution (<1.20 A) structure of a copper, protein, nitrite reductase, and of a mutant of the catalytically important, Asp92 residue (D92E). The atomic resolution where carbon-carbon bonds of, the peptide become clearly resolved, remains a key goal of structural, analysis. Despite much effort and technological progress, still very few, structures are known at such resolution. For example, in the Protein Data, Bank (PDB) there are some 200 structures of copper proteins but the, highest resolution structure is that of amicyanin, a small (12 kDa), protein, which has been resolved to 1.30 A. Here, we present the, structures of wild-type copper nitrite reductase (wtNiR) from Alcaligenes, xylosoxidans (36.5 kDa monomer), the "half-apo" recombinant native protein, ... | + | We provide the first atomic resolution (<1.20 A) structure of a copper, protein, nitrite reductase, and of a mutant of the catalytically important, Asp92 residue (D92E). The atomic resolution where carbon-carbon bonds of, the peptide become clearly resolved, remains a key goal of structural, analysis. Despite much effort and technological progress, still very few, structures are known at such resolution. For example, in the Protein Data, Bank (PDB) there are some 200 structures of copper proteins but the, highest resolution structure is that of amicyanin, a small (12 kDa), protein, which has been resolved to 1.30 A. Here, we present the, structures of wild-type copper nitrite reductase (wtNiR) from Alcaligenes, xylosoxidans (36.5 kDa monomer), the "half-apo" recombinant native protein, and the D92E mutant at 1.04, 1.15 and 1.12A resolutions, respectively., These structures provide the basis from which to build a detailed, mechanism of this important enzyme. |
==About this Structure== | ==About this Structure== | ||
| - | 1OE1 is a | + | 1OE1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans] with CU and PG4 as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OE1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: nitrite reductase]] | [[Category: nitrite reductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:27:32 2007'' |
Revision as of 11:22, 5 November 2007
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ATOMIC RESOLUTION STRUCTURE OF THE WILDTYPE NATIVE NITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS
Overview
We provide the first atomic resolution (<1.20 A) structure of a copper, protein, nitrite reductase, and of a mutant of the catalytically important, Asp92 residue (D92E). The atomic resolution where carbon-carbon bonds of, the peptide become clearly resolved, remains a key goal of structural, analysis. Despite much effort and technological progress, still very few, structures are known at such resolution. For example, in the Protein Data, Bank (PDB) there are some 200 structures of copper proteins but the, highest resolution structure is that of amicyanin, a small (12 kDa), protein, which has been resolved to 1.30 A. Here, we present the, structures of wild-type copper nitrite reductase (wtNiR) from Alcaligenes, xylosoxidans (36.5 kDa monomer), the "half-apo" recombinant native protein, and the D92E mutant at 1.04, 1.15 and 1.12A resolutions, respectively., These structures provide the basis from which to build a detailed, mechanism of this important enzyme.
About this Structure
1OE1 is a Single protein structure of sequence from Achromobacter xylosoxidans with CU and PG4 as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Atomic resolution structures of native copper nitrite reductase from Alcaligenes xylosoxidans and the active site mutant Asp92Glu., Ellis MJ, Dodd FE, Sawers G, Eady RR, Hasnain SS, J Mol Biol. 2003 Apr 25;328(2):429-38. PMID:12691751
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