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| | ==Crystal structure of D138N mutant of Drp35, a 35kDa drug responsive protein from Staphylococcus aureus== | | ==Crystal structure of D138N mutant of Drp35, a 35kDa drug responsive protein from Staphylococcus aureus== |
| - | <StructureSection load='2dso' size='340' side='right' caption='[[2dso]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='2dso' size='340' side='right'caption='[[2dso]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2dso]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DSO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DSO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2dso]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DSO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dg0|2dg0]], [[2dg1|2dg1]]</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=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,4-lactonase 1,4-lactonase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.25 3.1.1.25] </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=2dso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dso OCA], [https://pdbe.org/2dso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dso RCSB], [https://www.ebi.ac.uk/pdbsum/2dso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dso ProSAT]</span></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=2dso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dso OCA], [http://pdbe.org/2dso PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dso RCSB], [http://www.ebi.ac.uk/pdbsum/2dso PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dso ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DRP35_STAAM DRP35_STAAM]] Exhibits lactonase activity. Acts in cells with perturbed membrane integrity and is possibly related to the membrane homeostasis (By similarity). | + | [https://www.uniprot.org/uniprot/DRP35_STAAM DRP35_STAAM] Exhibits lactonase activity. Acts in cells with perturbed membrane integrity and is possibly related to the membrane homeostasis (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 1,4-lactonase]] | + | [[Category: Large Structures]] |
| - | [[Category: Morikawa, K]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Ohki, Y]] | + | [[Category: Morikawa K]] |
| - | [[Category: Ohta, T]] | + | [[Category: Ohki Y]] |
| - | [[Category: Tanaka, I]] | + | [[Category: Ohta T]] |
| - | [[Category: Tanaka, Y]] | + | [[Category: Tanaka I]] |
| - | [[Category: Watanabe, N]] | + | [[Category: Tanaka Y]] |
| - | [[Category: Yao, M]] | + | [[Category: Watanabe N]] |
| - | [[Category: Beta propeller]]
| + | [[Category: Yao M]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
DRP35_STAAM Exhibits lactonase activity. Acts in cells with perturbed membrane integrity and is possibly related to the membrane homeostasis (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Drp35 is a protein induced by cell wall-affecting antibiotics or detergents; it possesses calcium-dependent lactonase activity. To determine the molecular basis of the lactonase activity, we first solved the crystal structures of Drp35 with and without Ca(2+); these showed that the molecule has a six-bladed beta-propeller structure with two calcium ions bound at the center of the beta-propeller and surface region. Mutational analyses of evolutionarily conserved residues revealed that the central calcium-binding site is essential for the enzymatic activity of Drp35. Substitution of some other amino acid residues for the calcium-binding residues demonstrated the critical contributions of Glu(48), Asp(138), and Asp(236) to the enzymatic activity. Differential scanning calorimetric analysis revealed that the loss of activity of E48Q and D236N, but not D138N, was attributed to their inability to hold the calcium ion. Further structural analysis of the D138N mutant indicates that it lacks a water molecule bound to the calcium ion rather than the calcium ion itself. Based on these observations and structural information, a possible catalytic mechanism in which the calcium ion and its binding residues play direct roles was proposed for the lactonase activity of Drp35.
Structural and mutational analyses of Drp35 from Staphylococcus aureus: a possible mechanism for its lactonase activity.,Tanaka Y, Morikawa K, Ohki Y, Yao M, Tsumoto K, Watanabe N, Ohta T, Tanaka I J Biol Chem. 2007 Feb 23;282(8):5770-80. Epub 2006 Dec 13. PMID:17166853[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tanaka Y, Morikawa K, Ohki Y, Yao M, Tsumoto K, Watanabe N, Ohta T, Tanaka I. Structural and mutational analyses of Drp35 from Staphylococcus aureus: a possible mechanism for its lactonase activity. J Biol Chem. 2007 Feb 23;282(8):5770-80. Epub 2006 Dec 13. PMID:17166853 doi:10.1074/jbc.M607340200
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