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| | <StructureSection load='2zj6' size='340' side='right'caption='[[2zj6]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='2zj6' size='340' side='right'caption='[[2zj6]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zj6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._mis38 Pseudomonas sp. mis38]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZJ6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zj6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._MIS38 Pseudomonas sp. MIS38]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZJ6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2z8x|2z8x]], [[2z8z|2z8z]], [[2zj7|2zj7]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></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=2zj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zj6 OCA], [https://pdbe.org/2zj6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zj6 RCSB], [https://www.ebi.ac.uk/pdbsum/2zj6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zj6 ProSAT]</span></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=2zj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zj6 OCA], [https://pdbe.org/2zj6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zj6 RCSB], [https://www.ebi.ac.uk/pdbsum/2zj6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zj6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9RBY1_9PSED Q9RBY1_9PSED] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseudomonas sp. mis38]] | + | [[Category: Pseudomonas sp. MIS38]] |
| - | [[Category: Triacylglycerol lipase]]
| + | [[Category: Angkawidjaja C]] |
| - | [[Category: Angkawidjaja, C]] | + | [[Category: Kanaya S]] |
| - | [[Category: Kanaya, S]] | + | [[Category: Kuwahara K]] |
| - | [[Category: Kuwahara, K]] | + | |
| - | [[Category: Beta roll]]
| + | |
| - | [[Category: Calcium binding protein]]
| + | |
| - | [[Category: Calcium site mutant]]
| + | |
| - | [[Category: Family i 3 lipase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Rtx protein]]
| + | |
| Structural highlights
Function
Q9RBY1_9PSED
Publication Abstract from PubMed
A family I.3 lipase from Pseudomonas sp. MIS38 (PML) contains three Ca(2+)-binding sites (Ca1-Ca3) in the N-catalytic domain. Of them, the Ca1 site is formed only in an open conformation. To analyze the role of these Ca(2+)-binding sites, three mutant proteins D157A-PML, D275A-PML and D337A-PML, which are designed to remove the Ca1, Ca2 and Ca3 sites, respectively, were constructed. Of them, the crystal structures of D157A-PML and D337A-PML in a closed conformation were determined. Both structures are nearly identical to that of the wild-type protein, except that the Ca3 site is missing in the D337A-PML structure. D157A-PML was as stable as the wild-type protein. Nevertheless, it exhibited little lipase and very weak esterase activities. D275A-PML was less stable than the wild-type protein by approximately 5 degrees C in T(1/2). It exhibited weak but significant lipase and esterase activities when compared with the wild-type protein. D337A-PML was also less stable than the wild-type protein by approximately 5 degrees C in T(1/2) but was fully active. These results suggest that the Ca1 site is required to make the active site fully open by anchoring lid 1. The Ca2 and Ca3 sites contribute to the stabilization of PML. The Ca2 site is also required to make PML fully active.
Importance of the Ca2+-binding sites in the N-catalytic domain of a family I.3 lipase for activity and stability.,Kuwahara K, Angkawidjaja C, Matsumura H, Koga Y, Takano K, Kanaya S Protein Eng Des Sel. 2008 Dec;21(12):737-44. Epub 2008 Nov 5. PMID:18987131[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kuwahara K, Angkawidjaja C, Matsumura H, Koga Y, Takano K, Kanaya S. Importance of the Ca2+-binding sites in the N-catalytic domain of a family I.3 lipase for activity and stability. Protein Eng Des Sel. 2008 Dec;21(12):737-44. Epub 2008 Nov 5. PMID:18987131 doi:gzn057
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