1oe2: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
== | |||
==Atomic Resolution Structure of D92E Mutant of Alcaligenes xylosoxidans Nitrite Reductase== | |||
<StructureSection load='1oe2' size='340' side='right' caption='[[1oe2]], [[Resolution|resolution]] 1.12Å' scene=''> | <StructureSection load='1oe2' size='340' side='right' caption='[[1oe2]], [[Resolution|resolution]] 1.12Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| Line 6: | Line 7: | ||
<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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bq5|1bq5]], [[1gs6|1gs6]], [[1gs7|1gs7]], [[1gs8|1gs8]], [[1hau|1hau]], [[1haw|1haw]], [[1ndt|1ndt]], [[1oe1|1oe1]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bq5|1bq5]], [[1gs6|1gs6]], [[1gs7|1gs7]], [[1gs8|1gs8]], [[1hau|1hau]], [[1haw|1haw]], [[1ndt|1ndt]], [[1oe1|1oe1]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oe2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oe2 OCA], [http://pdbe.org/1oe2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oe2 RCSB], [http://www.ebi.ac.uk/pdbsum/1oe2 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oe2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oe2 OCA], [http://pdbe.org/1oe2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oe2 RCSB], [http://www.ebi.ac.uk/pdbsum/1oe2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oe2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 16: | Line 17: | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1oe2 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 27: | Line 28: | ||
</div> | </div> | ||
<div class="pdbe-citations 1oe2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1oe2" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:47, 1 November 2017
Atomic Resolution Structure of D92E Mutant of Alcaligenes xylosoxidans Nitrite ReductaseAtomic Resolution Structure of D92E Mutant of Alcaligenes xylosoxidans Nitrite Reductase
Structural highlights
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 PubMedWe 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 |
| ||||||||||||||||||||