1oe1: Difference between revisions
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[[Image:1oe1.gif|left|200px]]<br /><applet load="1oe1" size=" | [[Image:1oe1.gif|left|200px]]<br /><applet load="1oe1" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1oe1, resolution 1.04Å" /> | caption="1oe1, resolution 1.04Å" /> | ||
'''ATOMIC RESOLUTION STRUCTURE OF THE WILDTYPE NATIVE NITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS'''<br /> | '''ATOMIC RESOLUTION STRUCTURE OF THE WILDTYPE NATIVE NITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
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]. Known structural/functional Site: <scene name='pdbsite=AC1:Pg4 Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | 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 <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=PG4:'>PG4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Pg4+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.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:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:56:47 2008'' | ||
Revision as of 10:56, 3 February 2008
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ATOMIC RESOLUTION STRUCTURE OF THE WILDTYPE NATIVE NITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS
OverviewOverview
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 StructureAbout this Structure
1OE1 is a Single protein structure of sequence from Achromobacter xylosoxidans with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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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