1h70

<StructureSection load='1h70' size='340' side='right' caption='[[1h70]], [[Resolution|resolution]] 1.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[1h70]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H70 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H70 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIR:CITRULLINE'>CIR</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dimethylargininase Dimethylargininase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.18 3.5.3.18] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h70 OCA], [http://pdbe.org/1h70 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h70 RCSB], [http://www.ebi.ac.uk/pdbsum/1h70 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h70 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Nitric oxide synthase is inhibited by asymmetric NG-methylated derivatives of arginine whose cellular levels are controlled in part by dimethylarginine dimethylaminohydrolase (DDAH, EC 3.5.3.18). Levels of asymmetric NG,NG-dimethylarginine (ADMA) are known to correlate with certain disease states. Here, the first structure of a DDAH shows an unexpected similarity to arginine:glycine amidinotransferase (EC 2.1.4.1) and arginine deiminase (EC 3.5.3.6), thus defining a superfamily of arginine-modifying enzymes. The identification of a Cys-His-Glu catalytic triad and the structures of a Cys to Ser point mutant bound to both substrate and product suggest a reaction mechanism. Comparison of the ADMA-DDAH and arginine-amidinotransferase complexes reveals a dramatic rotation of the substrate that effectively maintains the orientation of the scissile bond of the substrate with respect to the catalytic residues. The DDAH structure will form a basis for the rational design of selective inhibitors, which are of potential use in modulating NO synthase activity in pathological settings.

Structural insights into the hydrolysis of cellular nitric oxide synthase inhibitors by dimethylarginine dimethylaminohydrolase.,Murray-Rust J, Leiper J, McAlister M, Phelan J, Tilley S, Santa Maria J, Vallance P, McDonald N Nat Struct Biol. 2001 Aug;8(8):679-83. PMID:11473257<ref>PMID:11473257</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1h70" style="background-color:#fffaf0;"></div>

==See Also==

*[[Dimethylarginine Dimethylaminohydrolase|Dimethylarginine Dimethylaminohydrolase]]

== References ==

<references/>

[[Category: Dimethylargininase]]

[[Category: Leiper, J]]

[[Category: McAlister, M]]

[[Category: McDonald, N]]

[[Category: Murray-Rust, J]]

[[Category: Phelan, J]]

[[Category: Santamaria, J]]

[[Category: Tilley, S]]

[[Category: Vallance, P]]

[[Category: Nitric oxide synthase inhibitor]]