1haw: Difference between revisions

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-{{Seed}}
-[[Image:1haw.png|left|200px]]
-<!--
+==X-RAY STRUCTURE OF A BLUE COPPER NITRITE REDUCTASE AT HIGH PH AND IN COPPER FREE FORM AT 1.9 A RESOLUTION==
-The line below this paragraph, containing "STRUCTURE_1haw", creates the "Structure Box" on the page.
+<StructureSection load='1haw' size='340' side='right'caption='[[1haw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1haw]] 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=1HAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HAW FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene></td></tr>
-{{STRUCTURE_1haw|  PDB=1haw  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1haw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1haw OCA], [https://pdbe.org/1haw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1haw RCSB], [https://www.ebi.ac.uk/pdbsum/1haw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1haw 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/ha/1haw_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=1haw ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Copper-containing nitrite reductases possess a trimeric structure where the catalytic Cu site, located at the monomer-monomer interface, resembles the catalytic sites of a number of Zn enzymes. Nitrite reductase from Alcaligenes xylosoxidans has optimum activity at pH 5.2 which decreases to a negligible level at pH 8. The structure of this nitrite reductase has previously been determined at pH 4.6. It has now been crystallized under new conditions at pH 8.5. Its crystallographic structure provides a structural explanation for the greatly reduced activity of the enzyme at high pH. Characterization of overexpressed protein in solution by EXAFS suggested that the protein lacked Cu in the catalytic type 2 Cu site and that the site was most probably occupied by Zn. Using the anomalous signals from Cu and Zn, the crystal structure revealed that the expressed protein was devoid of Cu in the catalytic site and that only a trace amount (&lt;10%) of Zn was present at this site in the crystal. Despite the close structural similarity of the catalytic site to a number of Zn enzymes, these data suggest that Zn, if it binds at the catalytic copper site, binds weakly in nitrite reductase.
-===X-RAY STRUCTURE OF A BLUE COPPER NITRITE REDUCTASE AT HIGH PH AND IN COPPER FREE FORM AT 1.9A RESOLUTION===
+X-ray structure of a blue copper nitrite reductase at high pH and in copper-free form at 1.9 A resolution.,Ellis MJ, Dodd FE, Strange RW, Prudencio M, Sawers G, Eady RR, Hasnain SS Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1110-8. Epub 2001, Jul 23. PMID:11468394<ref>PMID:11468394</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1haw" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_11468394}}, adds the Publication Abstract to the page
+*[[Nitrite reductase 3D structures|Nitrite reductase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 11468394 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11468394}}
+__TOC__
+</StructureSection>
-==About this Structure==
-HAW 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=1HAW OCA].
-==Reference==
-X-ray structure of a blue copper nitrite reductase at high pH and in copper-free form at 1.9 A resolution., Ellis MJ, Dodd FE, Strange RW, Prudencio M, Sawers G, Eady RR, Hasnain SS, Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1110-8. Epub 2001, Jul 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11468394 11468394]
 [[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: Prudencio, M.]]
+[[Category: Prudencio M]]
-[[Category: Sawerseady, R R.]]
+[[Category: Sawerseady RR]]
-[[Category: Strange, R W.]]
+[[Category: Strange RW]]
-[[Category: Blue copper]]
-[[Category: Copper]]
-[[Category: Nitrite reductase]]
-[[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 07:54:55 2008''