4cqd
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4cqd is ON HOLD Authors: Balotra, S., Newman, J., French, N.G., Peat, T.S., Scott, C. Description: The reaction mechanism of the N-isopropylammelid...) |
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The reaction mechanism of the N-isopropylammelide isopropylaminohydrolase AtzC: insights from structural and mutagenesis studies== |
| + | <StructureSection load='4cqd' size='340' side='right'caption='[[4cqd]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4cqd]] 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=4CQD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CQD 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]] 2.25Å</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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</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=4cqd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cqd OCA], [https://pdbe.org/4cqd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cqd RCSB], [https://www.ebi.ac.uk/pdbsum/4cqd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cqd 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4cqd" 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]] | ||
Current revision
The reaction mechanism of the N-isopropylammelide isopropylaminohydrolase AtzC: insights from structural and mutagenesis studies
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