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New page: left|200px<br /> <applet load="1wae" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wae, resolution 1.95Å" /> '''CRYSTAL STRUCTURE O... |
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== | ==Crystal structure of H129V Mutant of Alcaligenes Xylosoxidans Nitrite Reductase== | ||
Copper nitrite reductases contain both an electron-transfer type 1 Cu site | <StructureSection load='1wae' size='340' side='right'caption='[[1wae]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1wae]] 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=1WAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WAE 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]] 1.95Å</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=ZN:ZINC+ION'>ZN</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=1wae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wae OCA], [https://pdbe.org/1wae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wae RCSB], [https://www.ebi.ac.uk/pdbsum/1wae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wae 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/wa/1wae_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1wae ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Copper nitrite reductases contain both an electron-transfer type 1 Cu site and a catalytic type 2 Cu site. We have mutated one of the type 2 copper ligating histidines to observe the effect on catalytic turnover. This mutation has created a unique site where Cu is ligated by 2 His Nepsilon2 atoms alone. | |||
Observation of an unprecedented Cu Bis-His site: crystal structure of the H129V mutant of nitrite reductase.,Ellis MJ, Antonyuk SV, Strange RW, Sawers G, Eady RR, Hasnain SS Inorg Chem. 2004 Nov 29;43(24):7591-3. PMID:15554622<ref>PMID:15554622</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1wae" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Nitrite reductase 3D structures|Nitrite reductase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Achromobacter xylosoxidans]] | |||
[[Category: Large Structures]] | |||
[[Category: Antonyuk SV]] | |||
[[Category: Eady RR]] | |||
[[Category: Ellis MJ]] | |||
[[Category: Hasnain SS]] | |||
[[Category: Sawers G]] | |||
[[Category: Strange RW]] | |||
Latest revision as of 16:26, 13 December 2023
Crystal structure of H129V Mutant of Alcaligenes Xylosoxidans Nitrite ReductaseCrystal structure of H129V Mutant of Alcaligenes Xylosoxidans Nitrite Reductase
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCopper nitrite reductases contain both an electron-transfer type 1 Cu site and a catalytic type 2 Cu site. We have mutated one of the type 2 copper ligating histidines to observe the effect on catalytic turnover. This mutation has created a unique site where Cu is ligated by 2 His Nepsilon2 atoms alone. Observation of an unprecedented Cu Bis-His site: crystal structure of the H129V mutant of nitrite reductase.,Ellis MJ, Antonyuk SV, Strange RW, Sawers G, Eady RR, Hasnain SS Inorg Chem. 2004 Nov 29;43(24):7591-3. PMID:15554622[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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