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[[Image:1oe1.gif|left|200px]]<br />
<applet load="1oe1" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1oe1, resolution 1.04&Aring;" />
'''ATOMIC RESOLUTION STRUCTURE OF THE WILDTYPE NATIVE NITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS'''<br />


==Overview==
==Atomic Resolution Structure of the Wildtype Native Nitrite Reductase from Alcaligenes xylosoxidans==
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.
<StructureSection load='1oe1' size='340' side='right'caption='[[1oe1]], [[Resolution|resolution]] 1.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1oe1]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OE1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.04&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oe1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oe1 OCA], [https://pdbe.org/1oe1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oe1 RCSB], [https://www.ebi.ac.uk/pdbsum/1oe1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oe1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O68601_ALCXX O68601_ALCXX]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oe/1oe1_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oe1 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:12691751</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
<div class="pdbe-citations 1oe1" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Nitrite reductase 3D structures|Nitrite reductase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Achromobacter xylosoxidans]]
[[Category: Achromobacter xylosoxidans]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Dodd, F.E.]]
[[Category: Dodd FE]]
[[Category: Ellis, M.J.]]
[[Category: Ellis MJ]]
[[Category: Hasnain, S.S.]]
[[Category: Hasnain SS]]
[[Category: CU]]
[[Category: PG4]]
[[Category: denitrification]]
[[Category: nitrite reductase]]
 
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