1oe1: Difference between revisions
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|PDB= 1oe1 |SIZE=350|CAPTION= <scene name='initialview01'>1oe1</scene>, resolution 1.04Å | |PDB= 1oe1 |SIZE=350|CAPTION= <scene name='initialview01'>1oe1</scene>, resolution 1.04Å | ||
|SITE= <scene name='pdbsite=AC1:Pg4+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Pg4+Binding+Site+For+Chain+A'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oe1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oe1 OCA], [http://www.ebi.ac.uk/pdbsum/1oe1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oe1 RCSB]</span> | |||
}} | }} | ||
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[[Category: Ellis, M J.]] | [[Category: Ellis, M J.]] | ||
[[Category: Hasnain, S S.]] | [[Category: Hasnain, S S.]] | ||
[[Category: denitrification]] | [[Category: denitrification]] | ||
[[Category: nitrite reductase]] | [[Category: nitrite reductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:43:54 2008'' | ||
Revision as of 22:43, 30 March 2008
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| , resolution 1.04Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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