1oe3

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(New page: 200px<br /><applet load="1oe3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oe3, resolution 1.15&Aring;" /> '''ATOMIC RESOLUTION ST...)
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[[Image:1oe3.jpg|left|200px]]<br /><applet load="1oe3" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1oe3.jpg|left|200px]]<br /><applet load="1oe3" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1oe3, resolution 1.15&Aring;" />
caption="1oe3, resolution 1.15&Aring;" />
'''ATOMIC RESOLUTION STRUCTURE OF 'HALF APO' NIR'''<br />
'''ATOMIC RESOLUTION STRUCTURE OF 'HALF APO' NIR'''<br />
==Overview==
==Overview==
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We provide the first atomic resolution (&lt;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.
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We provide the first atomic resolution (&lt;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==
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1OE3 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]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OE3 OCA].
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1OE3 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 <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=PG4:'>PG4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OE3 OCA].
==Reference==
==Reference==
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[[Category: Achromobacter xylosoxidans]]
[[Category: Achromobacter xylosoxidans]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Dodd, F.E.]]
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[[Category: Dodd, F E.]]
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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.]]
[[Category: CU]]
[[Category: CU]]
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[[Category: nitrite reductase]]
[[Category: nitrite reductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:48:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:38 2008''

Revision as of 12:16, 21 February 2008


1oe3, resolution 1.15Å

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ATOMIC RESOLUTION STRUCTURE OF 'HALF APO' NIR

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

1OE3 is a Single protein structure of sequence from Achromobacter xylosoxidans with and as ligands. 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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