View source for 4cqc


==The reaction mechanism of the N-isopropylammelide isopropylaminohydrolase AtzC: insights from structural and mutagenesis studies==
<StructureSection load='4cqc' size='340' side='right'caption='[[4cqc]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4cqc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._ADP Pseudomonas sp. ADP]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CQC 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4cqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cqc OCA], [https://pdbe.org/4cqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cqc RCSB], [https://www.ebi.ac.uk/pdbsum/4cqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cqc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATZC_PSESD ATZC_PSESD] Transforms N-isopropylammelide to cyanuric acid and isopropylamine.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The N-isopropylammelide isopropylaminohydrolase from Pseudomonas sp. strain ADP, AtzC, provides the third hydrolytic step in the mineralization of s-triazine herbicides, such as atrazine. We obtained the X-ray crystal structure of AtzC at 1.84 A with a weak inhibitor bound in the active site and then used a combination of in silico docking and site-directed mutagenesis to understand the interactions between AtzC and its substrate, isopropylammelide. The substitution of an active site histidine residue (His249) for an alanine abolished the enzyme's catalytic activity. We propose a plausible catalytic mechanism, consistent with the biochemical and crystallographic data obtained that is similar to that found in carbonic anhydrase and other members of subtype III of the amidohydrolase family.

X-Ray Structure and Mutagenesis Studies of the N-Isopropylammelide Isopropylaminohydrolase, AtzC.,Balotra S, Warden AC, Newman J, Briggs LJ, Scott C, Peat TS PLoS One. 2015 Sep 21;10(9):e0137700. doi: 10.1371/journal.pone.0137700., eCollection 2015. PMID:26390431<ref>PMID:26390431</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4cqc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas sp. ADP]]
[[Category: Balotra S]]
[[Category: French NG]]
[[Category: Newman J]]
[[Category: Peat TS]]
[[Category: Scott C]]