2ci5: Difference between revisions

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-[[Image:2ci5.gif|left|200px]]<br />
-<applet load="2ci5" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2ci5, resolution 1.79&Aring;" />
-'''CRYSTAL STRUCTURE OF DIMETHYLARGININE DIMETHYLAMINOHYDROLASE I IN COMPLEX WITH L-HOMOCYSTEINE'''<br />
-==Overview==
+==Crystal structure of Dimethylarginine Dimethylaminohydrolase I in complex with L-homocysteine==
-Dimethylarginine dimethylaminohydrolase (DDAH) is involved in the, regulation of nitric oxide synthase (NOS) by metabolizing the free, endogenous arginine derivatives N(omega)-methyl-L-arginine (MMA) and, N(omega),N(omega)-dimethyl-L-arginine (ADMA), which are competitive, inhibitors of NOS. Here, we present high-resolution crystal structures of, DDAH isoform 1 (DDAH-1) isolated from bovine brain in complex with, different inhibitors, including S-nitroso-L-homocysteine and Zn2+, a, regulator of this mammalian enzyme. The structure of DDAH-1 consists of a, propeller-like fold similar to other arginine-modifying enzymes and a, flexible loop, which adopts different conformations and acts as a lid at, the entrance of the active site. The orientation and interaction mode of, inhibitors in the ... [[http://ispc.weizmann.ac.il/pmbin/getpm?16698551 (full description)]]
+<StructureSection load='2ci5' size='340' side='right'caption='[[2ci5]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
+== Structural highlights ==
-==About this Structure==
+<table><tr><td colspan='2'>[[2ci5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CI5 FirstGlance]. <br>
-CI5 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]] with HCS and CIT as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.18 3.5.3.18]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CI5 OCA]].
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene></td></tr>
-==Reference==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ci5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ci5 OCA], [https://pdbe.org/2ci5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ci5 RCSB], [https://www.ebi.ac.uk/pdbsum/2ci5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ci5 ProSAT]</span></td></tr>
-Structure of the mammalian NOS regulator dimethylarginine dimethylaminohydrolase: A basis for the design of specific inhibitors., Frey D, Braun O, Briand C, Vasak M, Grutter MG, Structure. 2006 May;14(5):901-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16698551 16698551]
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DDAH1_BOVIN DDAH1_BOVIN] Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
+== 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/ci/2ci5_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=2ci5 ConSurf].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
 [[Category: Bos taurus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Braun, O.]]
+[[Category: Braun O]]
-[[Category: Briand, C.]]
+[[Category: Briand C]]
-[[Category: Frey, D.]]
+[[Category: Frey D]]
-[[Category: Grutter, M.G.]]
+[[Category: Grutter MG]]
-[[Category: Vasak, M.]]
+[[Category: Vasak M]]
-[[Category: CIT]]
-[[Category: HCS]]
-[[Category: acetylation]]
-[[Category: adma]]
-[[Category: hydrolase]]
-[[Category: metal-binding]]
-[[Category: mma]]
-[[Category: no]]
-[[Category: nos regulation]]
-[[Category: s-nitrosylation]]
-[[Category: zinc]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:40:09 2007''