{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T07:36:14Z","timestamp":1792136174047,"version":"4.4.0"},"reference-count":38,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2005,11,14]],"date-time":"2005-11-14T00:00:00Z","timestamp":1131926400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2006,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The crystal structure of the phospholipase A2 (PLA<jats:sub>2<\/jats:sub>) heterodimer from <jats:italic>Naja naja sagittifera<\/jats:italic> reveals the presence of a new PLA<jats:sub>2<\/jats:sub>\u2010like protein with eight disulphide bridges. The heterodimer is formed between a commonly observed group I PLA<jats:sub>2<\/jats:sub> having seven characteristic disulfide bonds and a novel PLA<jats:sub>2<\/jats:sub>\u2010like protein (Cys\u2013PLA<jats:sub>2<\/jats:sub>) containing two extra cysteines at two highly conserved sites (positions 32 and 49) of structural and functional importantance. The crystals of the heterodimer belong to tetragonal space group P41212 with cell dimensions, <jats:italic>a<\/jats:italic> = <jats:italic>b<\/jats:italic> = 77.7 \u00c5 and <jats:italic>c<\/jats:italic> = 68.4 \u00c5 corresponding to a solvent content of 33%, which is one of the lowest values observed so far in the PLA<jats:sub>2<\/jats:sub> crystals. The structure has been solved with molecular replacement method and refined to a final <jats:italic>R<\/jats:italic> value of 21.6% [<jats:italic>R<\/jats:italic><jats:sub>free<\/jats:sub> = 25.6%]. The electron density revealed the presence of cysteines 32 and 49 that are covalently linked to give rise to an eighth disulphide bridge in the PLA<jats:sub>2<\/jats:sub>\u2010like monomer. A non\u2010protein high\u2010quality electron density was also observed at the substrate\u2010binding site in the PLA<jats:sub>2<\/jats:sub>\u2010like protein that has been interpreted as <jats:italic>N<\/jats:italic>\u2010acetylglucosamine. The overall tertiary folds of the two monomers are similar having all features of PLA<jats:sub>2<\/jats:sub>\u2010type folding. A zinc ion is detected at the interface of the heterodimer with fivefold coordination while another zinc ion was found on the surface of Cys\u2013PLA<jats:sub>2<\/jats:sub> with sixfold coordination. The conformations of the calcium\u2010binding loops of both monomers are significantly different from each other as well as from those in other group I PLA<jats:sub>2<\/jats:sub>s. The <jats:italic>N<\/jats:italic>\u2010acetylglucosamine molecule is favorably placed in the substrate\u2010binding site of Cys\u2013PLA<jats:sub>2<\/jats:sub> and forms five hydrogen bonds and several van der Waals interactions with protein atoms, thus indicating a strong affinity. It also provides clue of the possible mechanism of sugar recognition by PLA<jats:sub>2<\/jats:sub> and PLA2\u2010like proteins. The formation of heterodimer seems to have been induced by zinc ion. Proteins 2006. \u00a9 2005 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/prot.20708","type":"journal-article","created":{"date-parts":[[2005,11,16]],"date-time":"2005-11-16T23:51:06Z","timestamp":1132185066000},"page":"329-337","source":"Crossref","is-referenced-by-count":13,"title":["Crystal structure of a heterodimer of phospholipase A2 from <i>Naja naja sagittifera<\/i> at 2.3 \u00c5 resolution reveals the presence of a new PLA<sub>2<\/sub>\u2010like protein with a novel cys 32\u2013Cys 49 disulphide bridge with a bound sugar at the substrate\u2010binding site"],"prefix":"10.1002","volume":"62","author":[{"given":"Talat","family":"Jabeen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nagendra","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rajendra K.","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jayasankar","family":"Jasti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sujata","family":"Sharma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Punit","family":"Kaur","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alagiri","family":"Srinivasan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tej P.","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2005,11,14]]},"reference":[{"key":"e_1_2_5_2_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1983.tb07860.x"},{"key":"e_1_2_5_3_2","doi-asserted-by":"crossref","first-page":"17649","DOI":"10.1016\/S0021-9258(18)38213-9","article-title":"The crystal structure of a lysine 49 phospholipase A2 from the venom of the cottonmouth snake at 2.0 \u00c5 resolution","volume":"265","author":"Holland DR","year":"1990","journal-title":"J Biol Chem"},{"key":"e_1_2_5_4_2","doi-asserted-by":"publisher","DOI":"10.1006\/abbi.1999.1210"},{"key":"e_1_2_5_5_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M305210200"},{"key":"e_1_2_5_6_2","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1042\/bj3190961","article-title":"Asp\u201049 is not an absolute prerequisite for the enzymic activity of low\u2010M(r) phospholipases A2: purification, characterization and computer modelling of an enzymically active Ser\u201049 phospholipase A2, ecarpholin S, from the venom of Echis carinatus sochureki (saw\u2010scaled viper)","volume":"319","author":"Polgar J","year":"1996","journal-title":"Biochem J"},{"key":"e_1_2_5_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2744(76)90329-6"},{"key":"e_1_2_5_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0969-2126(01)00246-5"},{"key":"e_1_2_5_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-5793(97)00853-3"},{"key":"e_1_2_5_10_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1998.1987"},{"key":"e_1_2_5_11_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(87)90021-2"},{"key":"e_1_2_5_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(84)90786-3"},{"key":"e_1_2_5_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(85)90348-3"},{"key":"e_1_2_5_14_2","doi-asserted-by":"publisher","DOI":"10.1002\/bit.260120606"},{"key":"e_1_2_5_15_2","unstructured":"SchulzeT.Ein Echtzeitsystem zur Messung der dynamischen Lichtstreuung in Fl\u00fcssigkeiten. 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