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| | <StructureSection load='2qhe' size='340' side='right'caption='[[2qhe]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2qhe' size='340' side='right'caption='[[2qhe]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2qhe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Echca Echca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QHE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2qhe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Echis_carinatus Echis carinatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QHE FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2qhd|2qhd]], [[2qhg|2qhg]]</div></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]] 2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </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=2qhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qhe OCA], [https://pdbe.org/2qhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qhe RCSB], [https://www.ebi.ac.uk/pdbsum/2qhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qhe 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=2qhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qhe OCA], [https://pdbe.org/2qhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qhe RCSB], [https://www.ebi.ac.uk/pdbsum/2qhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qhe ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PA2HS_ECHCA PA2HS_ECHCA] |
| | == 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: Echca]] | + | [[Category: Echis carinatus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Go, M L]] | + | [[Category: Go ML]] |
| - | [[Category: Kini, R M]] | + | [[Category: Kini RM]] |
| - | [[Category: Sivaraman, J]] | + | [[Category: Sivaraman J]] |
| - | [[Category: Valiyaveettil, S]] | + | [[Category: Valiyaveettil S]] |
| - | [[Category: Zhou, X]] | + | [[Category: Zhou X]] |
| - | [[Category: Beta sheet]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Three helice]]
| + | |
| Structural highlights
Function
PA2HS_ECHCA
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
Phospholipase A(2) (PLA(2)), a common toxic component of snake venom, has been implicated in various pharmacological effects. Ecarpholin S, isolated from the venom of the snake Echis carinatus sochureki, is a phospholipase A(2) (PLA(2)) belonging to the Ser(49)-PLA(2) subgroup. It has been characterized as having low enzymatic but potent myotoxic activities. The crystal structures of native ecarpholin S and its complexes with lauric acid, and its inhibitor suramin, were elucidated. This is the first report of the structure of a member of the Ser(49)-PLA(2) subgroup. We also examined interactions of ecarpholin S with phosphatidylglycerol and lauric acid, using surface plasmon resonance, and of suramin with isothermal titration calorimetry. Most Ca(2+)-dependent PLA(2) enzymes have Asp in position 49, which plays a crucial role in Ca(2+) binding. The three-dimensional structure of ecarpholin S reveals a unique conformation of the Ca(2+)-binding loop that is not favorable for Ca(2+) coordination. Furthermore, the endogenously bound fatty acid (lauric acid) in the hydrophobic channel may also interrupt the catalytic cycle. These two observations may account for the low enzymatic activity of ecarpholin S, despite full retention of the catalytic machinery. These observations may also be applicable to other non-Asp(49)-PLA(2) enzymes. The interaction of suramin in its complex with ecarpholin S is quite different from that reported for the Lys(49)-PLA(2)/suramin complex(,) where the interfacial recognition face (i-face), C-terminal region, and N-terminal region of ecarpholin S play important roles. This study provides significant structural and functional insights into the myotoxic activity of ecarpholin S and, in general, of non-Asp(49)-PLA(2) enzymes.
Structural characterization of myotoxic ecarpholin S from Echis carinatus venom.,Zhou X, Tan TC, Valiyaveettil S, Go ML, Kini RM, Velazquez-Campoy A, Sivaraman J Biophys J. 2008 Oct;95(7):3366-80. Epub 2008 Jun 27. PMID:18586854[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhou X, Tan TC, Valiyaveettil S, Go ML, Kini RM, Velazquez-Campoy A, Sivaraman J. Structural characterization of myotoxic ecarpholin S from Echis carinatus venom. Biophys J. 2008 Oct;95(7):3366-80. Epub 2008 Jun 27. PMID:18586854 doi:10.1529/biophysj.107.117747
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