2ci5

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(New page: 200px<br /> <applet load="2ci5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ci5, resolution 1.79&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:2ci5.gif|left|200px]]<br />
 
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<applet load="2ci5" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ci5, resolution 1.79&Aring;" />
 
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'''CRYSTAL STRUCTURE OF DIMETHYLARGININE DIMETHYLAMINOHYDROLASE I IN COMPLEX WITH L-HOMOCYSTEINE'''<br />
 
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==Overview==
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==Crystal structure of Dimethylarginine Dimethylaminohydrolase I in complex with L-homocysteine==
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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)]]
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<StructureSection load='2ci5' size='340' side='right'caption='[[2ci5]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<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>
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2CI5 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]].
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</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>
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<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>
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==Reference==
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<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>
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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]
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ci/2ci5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Braun, O.]]
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[[Category: Braun O]]
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[[Category: Briand, C.]]
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[[Category: Briand C]]
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[[Category: Frey, D.]]
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[[Category: Frey D]]
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[[Category: Grutter, M.G.]]
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[[Category: Grutter MG]]
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[[Category: Vasak, M.]]
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[[Category: Vasak M]]
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[[Category: CIT]]
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[[Category: HCS]]
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[[Category: acetylation]]
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[[Category: adma]]
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[[Category: hydrolase]]
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[[Category: metal-binding]]
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[[Category: mma]]
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[[Category: no]]
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[[Category: nos regulation]]
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[[Category: s-nitrosylation]]
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[[Category: zinc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:40:09 2007''
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Current revision

Crystal structure of Dimethylarginine Dimethylaminohydrolase I in complex with L-homocysteine

PDB ID 2ci5

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