{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,20]],"date-time":"2026-05-20T11:54:19Z","timestamp":1779278059576,"version":"3.51.4"},"reference-count":0,"publisher":"International Union of Crystallography (IUCr)","issue":"11","license":[{"start":{"date-parts":[[1999,11,1]],"date-time":"1999-11-01T00:00:00Z","timestamp":941414400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[1999,11,1]],"date-time":"1999-11-01T00:00:00Z","timestamp":941414400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html#TDM"}],"content-domain":{"domain":["iucr.org","wiley.com","iucrj.org"],"crossmark-restriction":true},"short-container-title":["Acta Crystallogr D Biol Crystallogr","Acta Cryst D","Acta Cryst Sect D","Acta Crystallogr D","Acta Crystallogr Sect D","Acta Crystallogr Sect D Biol Crystallogr","Acta Crystallogr D Biol Cryst"],"published-print":{"date-parts":[[1999,11,1]]},"abstract":"<jats:p>The structure of acutolysin-C, a haemorrhagic zinc metalloproteinase from the venom of <jats:italic>Agkistrodon acutus<\/jats:italic>, has been analyzed and refined at 2.2\u2005\u00c5 resolution. The space group of the crystal is <jats:italic>P<\/jats:italic>2<jats:sub>1<\/jats:sub>2<jats:sub>1<\/jats:sub>2<jats:sub>1<\/jats:sub>, with unit-cell dimensions <jats:italic>a<\/jats:italic> = 46.84, <jats:italic>b<\/jats:italic>\u00a0=\u00a049.52, <jats:italic>c<\/jats:italic> = 95.34\u2005\u00c5. One molecule was found in each asymmetric unit. The phasing problem was solved by the molecular-replacement program <jats:italic>AMoRe<\/jats:italic>. Crystallographic refinement was performed using <jats:italic>X-PLOR<\/jats:italic>, leading to final <jats:italic>R<\/jats:italic> and free <jats:italic>R<\/jats:italic> factors of 0.176 and 0.272, respectively. The residue sequence of acutolysin-C was determined mainly by electron density. No density was found for the first residue at the N-terminus and the last two residues at the C-terminus, which was also the case for most other P-I class snake-venom metalloproteinases (SVMPs). Acutolysin-C has two highly conserved characteristic sequences His142-Glu143-<jats:italic>X<\/jats:italic>-<jats:italic>X<\/jats:italic>-His146-<jats:italic>X<\/jats:italic>-<jats:italic>X<\/jats:italic>-Gly149-<jats:italic>X<\/jats:italic>-<jats:italic>X<\/jats:italic>-His152 and Cys162-Ile163-Met164. The enzyme has three disulfide bridges: Cys117\u2013Cys195, Cys157\u2013Cys179 and Cys159\u2013Cys162. The entire structure shows good agreement with that of other reported P-I class SVMPs and has two subdomains with a cleft in which one catalytic zinc ion is localized. However, the local conformation (especially the disulfide configurations), the coordination of the catalytic water molecules and some residue side chains differ compared with other P-I class SVMPs. The proteolytic activities of SVMPs are sensitive to the pH value. The molecular superpositions around the proteolytic active sites of all the P-I class SVMP crystal structures show that the distances between the zinc ion and its ligands are not correlated with the crystallization pH values, although the contact distances between the catalytic water molecule and the O atoms of the Glu143 carboxylate group in the neutral and weakly alkaline structures are shorter than those in weakly acidic structures, and the closer the crystallization pH value of one enzyme is to its optimal activity pH value, the shorter the contact distances. Overall, all P-I class SVMPs have similar conformations in the active-site cleft. The size of the active site is not correlated with the crystallization pH values or the proteolytic activities. The disulfide bridge Cys117\u2013Cys195 is conserved in all crystal structures of P-I class SVMPs, whereas the conformation and number of disulfide bridges in the C-terminal subdomain differ. Acutolysin-C has no structural calcium ion, which may not affect the proteolytic activity or haemorrhagic activity directly.<\/jats:p>","DOI":"10.1107\/s0907444999010306","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T05:23:52Z","timestamp":1027747432000},"page":"1834-1841","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":30,"title":["Structure of acutolysin-C, a haemorrhagic toxin from the venom of <i>Agkistrodon acutus<\/i>, providing further evidence for the mechanism of the pH-dependent proteolytic reaction of zinc metalloproteinases"],"prefix":"10.1107","volume":"55","author":[{"given":"Xue-yong","family":"Zhu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mai-kun","family":"Teng","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Li-wen","family":"Niu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"329","published-online":{"date-parts":[[1999,11,1]]},"container-title":["Acta Crystallographica Section D Biological Crystallography"],"original-title":[],"link":[{"URL":"http:\/\/journals.iucr.org\/d\/issues\/1999\/11\/00\/gr0927\/gr0927.pdf","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/journals.iucr.org\/d\/issues\/1999\/11\/00\/gr0927\/gr0927.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,1,9]],"date-time":"2025-01-09T12:56:58Z","timestamp":1736427418000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.iucr.org\/paper?S0907444999010306"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1999,11,1]]},"references-count":0,"journal-issue":{"issue":"11","published-print":{"date-parts":[[1999,11]]}},"alternative-id":["S0907444999010306"],"URL":"https:\/\/doi.org\/10.1107\/s0907444999010306","relation":{},"ISSN":["0907-4449"],"issn-type":[{"value":"0907-4449","type":"print"}],"subject":[],"published":{"date-parts":[[1999,11,1]]},"assertion":[{"value":"Acta Crystallographica Section D: Biological Crystallography","order":0,"name":"journal","label":"Publication","explanation":{"URL":"http:\/\/journals.iucr.org\/d"},"group":{"name":"general","label":"General"}},{"value":"research papers","order":1,"name":"content_type","label":"Content type","explanation":{"URL":"http:\/\/journals.iucr.org\/d\/services\/notesforauthors.html"},"group":{"name":"general","label":"General"}},{"value":"Available","URL":"http:\/\/scripts.iucr.org\/cgi-bin\/citedin?gr0927","order":2,"name":"article_metrics","label":"Article metrics","group":{"name":"general","label":"General"}},{"value":"Yes","order":0,"name":"peer_reviewed","label":"Peer reviewed","group":{"name":"peer_review","label":"Peer review"}},{"value":"Single blind","order":1,"name":"review_process","label":"Review process","group":{"name":"peer_review","label":"Peer review"}},{"value":"8 March 1999","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication history"}},{"value":"27 July 1999","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication history"}},{"value":"1 November 1999","order":2,"name":"published_online","label":"Published online","group":{"name":"publication_history","label":"Publication history"}},{"value":"This article has supporting information","name":"supplementary_materials","label":"Supplementary materials","explanation":{"URL":"http:\/\/scripts.iucr.org\/cgi-bin\/sendsup?gr0927"}},{"value":"\u00a9 1999 International Union of Crystallography","order":0,"name":"copyright","label":"Copyright","explanation":{"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},"group":{"name":"copyright_and_licensing","label":"Copyright and licencing"}}]}}