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1oe2

From Proteopedia

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Atomic Resolution Structure of D92E Mutant of Alcaligenes xylosoxidans Nitrite Reductase

Structural highlights

1oe2 is a 1 chain structure with sequence from Achromobacter xylosoxidans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.12Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

O68601_ALCXX

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ellis MJ, Dodd FE, Sawers G, Eady RR, Hasnain SS. Atomic resolution structures of native copper nitrite reductase from Alcaligenes xylosoxidans and the active site mutant Asp92Glu. J Mol Biol. 2003 Apr 25;328(2):429-38. PMID:12691751

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1oe2"

@@ Line 3: / Line 3: @@
 <StructureSection load='1oe2' size='340' side='right'caption='[[1oe2]], [[Resolution|resolution]] 1.12&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1oe2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"achromobacter_xylosoxidans"_yabuuchi_and_ohyama_1971 "achromobacter xylosoxidans" yabuuchi and ohyama 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OE2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1oe2]] 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=1OE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OE2 FirstGlance]. <br>
-</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=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.12&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bq5|1bq5]], [[1gs6|1gs6]], [[1gs7|1gs7]], [[1gs8|1gs8]], [[1hau|1hau]], [[1haw|1haw]], [[1ndt|1ndt]], [[1oe1|1oe1]]</div></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=1oe2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oe2 OCA], [https://pdbe.org/1oe2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oe2 RCSB], [https://www.ebi.ac.uk/pdbsum/1oe2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oe2 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/O68601_ALCXX O68601_ALCXX]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Achromobacter xylosoxidans yabuuchi and ohyama 1971]]
+[[Category: Achromobacter xylosoxidans]]
 [[Category: Large Structures]]
-[[Category: Dodd, F E]]
+[[Category: Dodd FE]]
-[[Category: Eady, R R]]
+[[Category: Eady RR]]
-[[Category: Ellis, M J]]
+[[Category: Ellis MJ]]
-[[Category: Hasnain, S S]]
+[[Category: Hasnain SS]]
-[[Category: Sawers, G]]
+[[Category: Sawers G]]
-[[Category: Copper protein]]
-[[Category: Nitrite reductase]]
-[[Category: Reductase]]

1oe2

From Proteopedia

Current revision

Atomic Resolution Structure of D92E Mutant of Alcaligenes xylosoxidans Nitrite Reductase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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