1oe1: Difference between revisions

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[[Image:1oe1.gif|left|200px]]<br /><applet load="1oe1" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1oe1.gif|left|200px]]
caption="1oe1, resolution 1.04&Aring;" />
 
'''ATOMIC RESOLUTION STRUCTURE OF THE WILDTYPE NATIVE NITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS'''<br />
{{Structure
|PDB= 1oe1 |SIZE=350|CAPTION= <scene name='initialview01'>1oe1</scene>, resolution 1.04&Aring;
|SITE= <scene name='pdbsite=AC1:Pg4+Binding+Site+For+Chain+A'>AC1</scene>
|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> and <scene name='pdbligand=PG4:TETRAETHYLENE GLYCOL'>PG4</scene>
|ACTIVITY=
|GENE=
}}
 
'''ATOMIC RESOLUTION STRUCTURE OF THE WILDTYPE NATIVE NITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS'''
 


==Overview==
==Overview==
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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 <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].  
1OE1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OE1 OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12691751 12691751]
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:[http://www.ncbi.nlm.nih.gov/pubmed/12691751 12691751]
[[Category: Achromobacter xylosoxidans]]
[[Category: Achromobacter xylosoxidans]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: nitrite reductase]]
[[Category: nitrite reductase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:35 2008''
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Revision as of 14:09, 20 March 2008

File:1oe1.gif


PDB ID 1oe1

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, resolution 1.04Å
Sites:
Ligands: and
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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