4tr2
From Proteopedia
(Difference between revisions)
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- | ''' | + | ==Crystal structure of PvSUB1== |
+ | <StructureSection load='4tr2' size='340' side='right' caption='[[4tr2]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4tr2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TR2 FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tr2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tr2 RCSB], [http://www.ebi.ac.uk/pdbsum/4tr2 PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The Plasmodium subtilase SUB1 plays a pivotal role during the egress of malaria parasites from host hepatocytes and erythrocytes. Here we report the crystal structure of full-length SUB1 from the human-infecting parasite Plasmodium vivax, revealing a bacterial-like catalytic domain in complex with a Plasmodium-specific prodomain. The latter displays a novel architecture with an amino-terminal insertion that functions as a 'belt', embracing the catalytic domain to further stabilize the quaternary structure of the pre-protease, and undergoes calcium-dependent autoprocessing during subsequent activation. Although dispensable for recombinant enzymatic activity, the SUB1 'belt' could not be deleted in Plasmodium berghei, suggesting an essential role of this domain for parasite development in vivo. The SUB1 structure not only provides a valuable platform to develop new anti-malarial candidates against this promising drug target, but also defines the Plasmodium-specific 'belt' domain as a key calcium-dependent regulator of SUB1 during parasite egress from host cells. | ||
- | + | A novel Plasmodium-specific prodomain fold regulates the malaria drug target SUB1 subtilase.,Giganti D, Bouillon A, Tawk L, Robert F, Martinez M, Crublet E, Weber P, Girard-Blanc C, Petres S, Haouz A, Hernandez JF, Mercereau-Puijalon O, Alzari PM, Barale JC Nat Commun. 2014 Sep 10;5:4833. doi: 10.1038/ncomms5833. PMID:25204226<ref>PMID:25204226</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Alzari, P M.]] | ||
+ | [[Category: Barale, J C.]] | ||
+ | [[Category: Bouillon, A.]] | ||
+ | [[Category: Giganti, D.]] | ||
+ | [[Category: Girard-Blanc, C.]] | ||
+ | [[Category: Haouz, A.]] | ||
+ | [[Category: Martinez, M.]] | ||
+ | [[Category: Petres, S.]] | ||
+ | [[Category: Weber, P.]] | ||
+ | [[Category: Calcium-binding]] | ||
+ | [[Category: Hydrolase]] | ||
+ | [[Category: Plasmodium egress protease]] |
Revision as of 06:40, 24 September 2014
Crystal structure of PvSUB1
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