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| | ==Crystal structure of the maleate isomerase Iso(C200A) from Pseudomonas putida S16 with maleate== | | ==Crystal structure of the maleate isomerase Iso(C200A) from Pseudomonas putida S16 with maleate== |
| - | <StructureSection load='4fq5' size='340' side='right' caption='[[4fq5]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='4fq5' size='340' side='right'caption='[[4fq5]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4fq5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Psep6 Psep6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FQ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FQ5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4fq5]] is a 2 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=4FQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FQ5 FirstGlance]. <br> |
| - | </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> | + | </td></tr><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> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fq7|4fq7]], [[4fuz|4fuz]]</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=4fq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fq5 OCA], [https://pdbe.org/4fq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fq5 RCSB], [https://www.ebi.ac.uk/pdbsum/4fq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fq5 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPS_4060 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1042876 PSEP6])</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=4fq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fq5 OCA], [http://pdbe.org/4fq5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fq5 RCSB], [http://www.ebi.ac.uk/pdbsum/4fq5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fq5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/F8G0M3_PSEP6 F8G0M3_PSEP6] Catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate.[HAMAP-Rule:MF_00943] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Psep6]] | + | [[Category: Large Structures]] |
| - | [[Category: Chen, D]] | + | [[Category: Pseudomonas putida S16]] |
| - | [[Category: Li, Q]] | + | [[Category: Chen D]] |
| - | [[Category: Lu, Y]] | + | [[Category: Li Q]] |
| - | [[Category: Wu, G]] | + | [[Category: Lu Y]] |
| - | [[Category: Xu, P]] | + | [[Category: Wu G]] |
| - | [[Category: Zhang, Z]] | + | [[Category: Xu P]] |
| - | [[Category: Isomerase]]
| + | [[Category: Zhang Z]] |
| - | [[Category: Maleate isomerase]]
| + | |
| Structural highlights
Function
F8G0M3_PSEP6 Catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate.[HAMAP-Rule:MF_00943]
Publication Abstract from PubMed
Nicotine is an environmental toxicant in tobacco waste, imposing a serious hazard for human health. Some bacteria including Pseudomonas spp. strains are able to metabolize nicotine to non-toxic compounds. The pyrrolidine pathway of nicotine degradation in Pseudomonas putida S16 has recently been revealed. The maleate isomerase (Pp-Iso) catalyses the last step in nicotine degradation of P. putida S16, the cis-trans isomerization of maleate to fumarate. In this study, we determined the crystal structures of both wild type isomerase by itself and its C200A point mutant in complex with its substrate maleate, to resolutions of 2.95 A and 2.10 A respectively. Our structures reveal that Asn17 and Asn169 play critical roles in recognizing the maleate by site-directed mutants' analysis. Surprisingly, our structure shows that the maleate is completely wrapped inside the isomerase. Examination of the structure prompted us to hypothesize that the beta2-alpha2 loop and the beta6-alpha7 loop have a breathing motion that regulates substrate/solvent entry and product departure. Our results of molecular dynamics simulation and enzymatic activity assay are fully consistent with this hypothesis. The isomerase probably uses this breathing motion to prevent the solvent from entering the active site and prohibit unproductive side reactions from happening.
Structural and computational studies of the maleate isomerase from Pseudomonas putida S16 reveal a breathing motion wrapping the substrate inside.,Chen D, Tang H, Lv Y, Zhang Z, Shen K, Lin K, Zhao YL, Wu G, Xu P Mol Microbiol. 2013 Mar;87(6):1237-44. doi: 10.1111/mmi.12163. Epub 2013 Feb 13. PMID:23347155[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen D, Tang H, Lv Y, Zhang Z, Shen K, Lin K, Zhao YL, Wu G, Xu P. Structural and computational studies of the maleate isomerase from Pseudomonas putida S16 reveal a breathing motion wrapping the substrate inside. Mol Microbiol. 2013 Mar;87(6):1237-44. doi: 10.1111/mmi.12163. Epub 2013 Feb 13. PMID:23347155 doi:10.1111/mmi.12163
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