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New page: '''Unreleased structure''' The entry 6luh is ON HOLD Authors: Oda, K., Matoba, Y. Description: High resolution structure of N(omega)-hydroxy-L-arginine hydrolase [[Category: Unreleased...
 
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'''Unreleased structure'''


The entry 6luh is ON HOLD
==High resolution structure of N(omega)-hydroxy-L-arginine hydrolase==
<StructureSection load='6luh' size='340' side='right'caption='[[6luh]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LUH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6luh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6luh OCA], [https://pdbe.org/6luh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6luh RCSB], [https://www.ebi.ac.uk/pdbsum/6luh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6luh ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DcsB, one of the enzymes encoded in the D-cycloserine (D-CS) biosynthetic gene cluster, displays a high sequence homology to arginase, which contains two manganese ions in the active site. However, DcsB hydrolyzes N(omega)-hydroxy-L-arginine, but not L-arginine, to supply hydroxyurea for the biosynthesis of D-CS. Here, the crystal structure of DcsB was determined at a resolution of 1.5 A using anomalous scattering from the manganese ions. In the crystal structure, DscB generates an artificial dimer created by the open and closed forms. Gel-filtration analysis demonstrated that DcsB is a monomeric protein, unlike arginase, which forms a trimeric structure. The active center containing the binuclear manganese cluster differs between DcsB and arginase. In DcsB, one of the ligands of the MnA ion is a cysteine, while the corresponding residue in arginase is a histidine. In addition, DcsB has no counterpart to the histidine residue that acts as a general acid/base during the catalytic reaction of arginase. The present study demonstrates that DcsB has a unique active site that differs from that of arginase.


Authors: Oda, K., Matoba, Y.
Crystal structure of an N(omega)-hydroxy-L-arginine hydrolase found in the D-cycloserine biosynthetic pathway.,Oda K, Shimotani N, Kuroda T, Matoba Y Acta Crystallogr D Struct Biol. 2020 Jun 1;76(Pt 6):506-514. doi:, 10.1107/S2059798320004908. Epub 2020 May 29. PMID:32496212<ref>PMID:32496212</ref>


Description: High resolution structure of N(omega)-hydroxy-L-arginine hydrolase
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Oda, K]]
<div class="pdbe-citations 6luh" style="background-color:#fffaf0;"></div>
[[Category: Matoba, Y]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Matoba Y]]
[[Category: Oda K]]
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