2not

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(New page: 200px<br /><applet load="2not" size="450" color="white" frame="true" align="right" spinBox="true" caption="2not, resolution 3.0&Aring;" /> '''NOTECHIS II-5, NEUROT...)
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[[Image:2not.gif|left|200px]]<br /><applet load="2not" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2not, resolution 3.0&Aring;" />
 
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'''NOTECHIS II-5, NEUROTOXIC PHOSPHOLIPASE A2 FROM NOTECHIS SCUTATUS SCUTATUS'''<br />
 
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==Overview==
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==NOTECHIS II-5, NEUROTOXIC PHOSPHOLIPASE A2 FROM NOTECHIS SCUTATUS SCUTATUS==
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The three-dimensional structures of the class II anticoagulant, phospholipase A2 (PLA2) toxin RVV-VD from the venom of Russell's viper, Vipera russelli russelli, and the class I neurotoxic PLA2 Notechis II-5, from the, Australian tiger snake, Notechis scutatus scutatus, were, determined to 2.2 A and 3.0 A resolution, respectively. Both enzymes are, monomeric and consist of 121 and 119 residues, respectively. A comparison, of ten class I/II PLA2 structures showed, among other differences, that, the beta-sheet of these enzymes (residues 76-83) is about 90 degrees less, twisted in class I than in class II PLA2s. This, along with the insertion, of some residues in the region 57-59 in class I enzymes (the elapid loop), could be the main reason for the significant difference in the, anticoagulant and (presynaptic) neurotoxic properties between the two, classes of PLA2. It seems apparent from sequence and structural, comparisons that the toxic site of PLA2 responsible for the strong, anticoagulancy of these toxins consists of a negatively charged part, Glu53, together with a positively charged ridge of lysine residues free, for intermolecular interactions. These lysines differ between the two, classes of PLA2.
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<StructureSection load='2not' size='340' side='right'caption='[[2not]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2not]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Notechis_scutatus_scutatus Notechis scutatus scutatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NOT FirstGlance]. <br>
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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]] 3&#8491;</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=2not FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2not OCA], [https://pdbe.org/2not PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2not RCSB], [https://www.ebi.ac.uk/pdbsum/2not PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2not ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PA2B5_NOTSC PA2B5_NOTSC] Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. Notechis II-5 is less toxic than notexin but has a higher specific phospholipase activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/no/2not_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2not ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The three-dimensional structures of the class II anticoagulant phospholipase A2 (PLA2) toxin RVV-VD from the venom of Russell's viper, Vipera russelli russelli, and the class I neurotoxic PLA2 Notechis II-5 from the, Australian tiger snake, Notechis scutatus scutatus, were determined to 2.2 A and 3.0 A resolution, respectively. Both enzymes are monomeric and consist of 121 and 119 residues, respectively. A comparison of ten class I/II PLA2 structures showed, among other differences, that the beta-sheet of these enzymes (residues 76-83) is about 90 degrees less twisted in class I than in class II PLA2s. This, along with the insertion of some residues in the region 57-59 in class I enzymes (the elapid loop), could be the main reason for the significant difference in the anticoagulant and (presynaptic) neurotoxic properties between the two classes of PLA2. It seems apparent from sequence and structural comparisons that the toxic site of PLA2 responsible for the strong anticoagulancy of these toxins consists of a negatively charged part, Glu53, together with a positively charged ridge of lysine residues free for intermolecular interactions. These lysines differ between the two classes of PLA2.
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==About this Structure==
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The three-dimensional structures of two toxins from snake venom throw light on the anticoagulant and neurotoxic sites of phospholipase A2.,Carredano E, Westerlund B, Persson B, Saarinen M, Ramaswamy S, Eaker D, Eklund H Toxicon. 1998 Jan;36(1):75-92. PMID:9604284<ref>PMID:9604284</ref>
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2NOT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Notechis_scutatus_scutatus Notechis scutatus scutatus]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NOT OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The three-dimensional structures of two toxins from snake venom throw light on the anticoagulant and neurotoxic sites of phospholipase A2., Carredano E, Westerlund B, Persson B, Saarinen M, Ramaswamy S, Eaker D, Eklund H, Toxicon. 1998 Jan;36(1):75-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9604284 9604284]
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</div>
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[[Category: Notechis scutatus scutatus]]
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<div class="pdbe-citations 2not" style="background-color:#fffaf0;"></div>
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[[Category: Phospholipase A(2)]]
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[[Category: Single protein]]
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[[Category: Carredano, E.]]
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[[Category: Eaker, D.]]
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[[Category: Eklund, H.]]
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[[Category: Persson, B.]]
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[[Category: Ramaswamy, S.]]
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[[Category: Saarinen, M.]]
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[[Category: Westerlund, B.]]
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[[Category: calcium]]
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[[Category: hydrolase]]
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[[Category: lipid degradation]]
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[[Category: presynaptic neurotoxin]]
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[[Category: venom]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:49:14 2007''
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==See Also==
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*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Notechis scutatus scutatus]]
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[[Category: Carredano E]]
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[[Category: Eaker D]]
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[[Category: Eklund H]]
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[[Category: Persson B]]
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[[Category: Ramaswamy S]]
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[[Category: Saarinen M]]
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[[Category: Westerlund B]]

Current revision

NOTECHIS II-5, NEUROTOXIC PHOSPHOLIPASE A2 FROM NOTECHIS SCUTATUS SCUTATUS

PDB ID 2not

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