4l08

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==Crystal structure of the maleamate amidase Ami(C149A) in complex with maleate from Pseudomonas putida S16==
==Crystal structure of the maleamate amidase Ami(C149A) in complex with maleate from Pseudomonas putida S16==
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<StructureSection load='4l08' size='340' side='right' caption='[[4l08]], [[Resolution|resolution]] 2.66&Aring;' scene=''>
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<StructureSection load='4l08' size='340' side='right'caption='[[4l08]], [[Resolution|resolution]] 2.66&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4l08]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L08 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L08 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4l08]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_S16 Pseudomonas putida S16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L08 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L08 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAE:MALEIC+ACID'>MAE</scene></td></tr>
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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]] 2.66&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l07|4l07]]</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=MAE:MALEIC+ACID'>MAE</scene></td></tr>
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<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=4l08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l08 OCA], [http://pdbe.org/4l08 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l08 RCSB], [http://www.ebi.ac.uk/pdbsum/4l08 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l08 ProSAT]</span></td></tr>
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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=4l08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l08 OCA], [https://pdbe.org/4l08 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l08 RCSB], [https://www.ebi.ac.uk/pdbsum/4l08 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l08 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/F8G0M0_PSEP6 F8G0M0_PSEP6]
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N-heterocyclic compounds from industrial wastes, including nicotine, are environmental pollutants or toxicants responsible for a variety of health problems. Microbial biodegradation is an attractive strategy for the removal of N-heterocyclic pollutants, during which carbon-nitrogen bonds in N-heterocycles are converted to amide bonds and subsequently severed by amide hydrolases. Previous studies have failed to clarify the molecular mechanism through which amide hydrolases selectively recognize diverse amide substrates and complete the biodenitrogenation process. In this study, structural, computational and enzymatic analyses showed how the N-formylmaleamate deformylase Nfo and the maleamate amidase Ami, two pivotal amide hydrolases in the nicotine catabolic pathway of Pseudomonas putida S16, specifically recognize their respective substrates. In addition, comparison of the alpha-beta-alpha groups of amidases, which include Ami, pinpointed several subgroup-characteristic residues differentiating the two classes of amide substrates as containing either carboxylate groups or aromatic rings. Furthermore, this study reveals the molecular mechanism through which the specially tailored active sites of deformylases and amidases selectively recognize their unique substrates. Our work thus provides a thorough elucidation of the molecular mechanism through which amide hydrolases accomplish substrate-specific recognition in the microbial N-heterocycles biodenitrogenation pathway.
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Structural insights into the specific recognition of N-heterocycle biodenitrogenation-derived substrates by microbial amide hydrolases.,Wu G, Chen D, Tang H, Ren Y, Chen Q, Lv Y, Zhang Z, Zhao YL, Yao Y, Xu P Mol Microbiol. 2014 Mar;91(5):1009-21. doi: 10.1111/mmi.12511. Epub 2014 Jan 23. PMID:24397579<ref>PMID:24397579</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4l08" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chen, D D]]
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[[Category: Large Structures]]
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[[Category: Lu, Y]]
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[[Category: Pseudomonas putida S16]]
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[[Category: Wu, G]]
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[[Category: Chen DD]]
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[[Category: Xu, P]]
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[[Category: Lu Y]]
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[[Category: Zhang, Z]]
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[[Category: Wu G]]
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[[Category: Hydrolase]]
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[[Category: Xu P]]
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[[Category: Maleamate amidase]]
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[[Category: Zhang Z]]

Current revision

Crystal structure of the maleamate amidase Ami(C149A) in complex with maleate from Pseudomonas putida S16

PDB ID 4l08

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