1oqc: Difference between revisions

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-{{Seed}}
-[[Image:1oqc.png|left|200px]]
-<!--
+==The crystal structure of augmenter of liver regeneration: a mammalian FAD dependent sulfhydryl oxidase==
-The line below this paragraph, containing "STRUCTURE_1oqc", creates the "Structure Box" on the page.
+<StructureSection load='1oqc' size='340' side='right'caption='[[1oqc]], [[Resolution|resolution]] 1.80&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'>[[1oqc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OQC 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]] 1.8&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-{{STRUCTURE_1oqc|  PDB=1oqc  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oqc OCA], [https://pdbe.org/1oqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oqc RCSB], [https://www.ebi.ac.uk/pdbsum/1oqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oqc ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ALR_RAT ALR_RAT] FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Within the mitochondrial intermembrane space, participates in a chain of disulfide exchange reactions with MIA40, that generate disulfide bonds in a number of resident proteins with twin Cx3C and Cx9C motifs. May have a function in liver regeneration and spermatogenesis.<ref>PMID:8058770</ref>
+== 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/oq/1oqc_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=1oqc ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The crystal structure of recombinant rat augmenter of liver regeneration (ALRp) has been determined to 1.8 A. The protein is a homodimer, stabilized by extensive noncovalent interactions and a network of hydrogen bonds, and possesses a noncovalently bound FAD in a motif previously found only in the related protein ERV2p. ALRp functions in vitro as a disulfide oxidase using dithiothreitol as reductant. Reduction of the flavin by DTT occurs under aerobic conditions resulting in a spectrum characteristic of a neutral semiquinone. This semiquinone is stable and is only fully reduced by addition of dithionite. Mutation of either of two cysteine residues that are located adjacent to the FAD results in inactivation of the oxidase activity. A comparison of ALRp with ERV2p is made that reveals a number of significant structural differences, which are related to the in vivo functions of these two proteins. Possible physiological roles of ALR are examined and a hypothesis that it may serve multiple roles is proposed.
-===The crystal structure of augmenter of liver regeneration: a mammalian FAD dependent sulfhydryl oxidase===
+The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase.,Wu CK, Dailey TA, Dailey HA, Wang BC, Rose JP Protein Sci. 2003 May;12(5):1109-18. PMID:012717032<ref>PMID:012717032</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-==About this Structure==
+</div>
-OQC is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQC OCA].
+<div class="pdbe-citations 1oqc" style="background-color:#fffaf0;"></div>
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:12717032</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Rattus norvegicus]]
-[[Category: Rose, J P.]]
+[[Category: Rose JP]]
-[[Category: Wang, B C.]]
+[[Category: Wang B-C]]
-[[Category: Wu, C K.]]
+[[Category: Wu C-K]]
-[[Category: Alr]]
-[[Category: Helix-turn-helix]]
-[[Category: Liver regeneration]]
-[[Category: Sulfhydryl oxidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 19:39:14 2009''