5bwy
From Proteopedia
(Difference between revisions)
| (5 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structure of proplasmepsin II from Plasmodium falciparum, Space Group P43212== | |
| + | <StructureSection load='5bwy' size='340' side='right'caption='[[5bwy]], [[Resolution|resolution]] 2.64Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5bwy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BWY FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.644Å</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=5bwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bwy OCA], [https://pdbe.org/5bwy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bwy RCSB], [https://www.ebi.ac.uk/pdbsum/5bwy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bwy ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PLM2_PLAFX PLM2_PLAFX] During the asexual blood stage, participates in initial cleavage of native host hemoglobin (Hb) resulting in Hb denaturation (PubMed:11782538, PubMed:15574427, PubMed:8844673). May cleave preferentially denatured hemoglobin that has been cleaved by PMI (PubMed:8844673). Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity (Probable).<ref>PMID:11782538</ref> <ref>PMID:15574427</ref> <ref>PMID:8844673</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Plasmepsin IV from Plasmodium falciparum (PM IV) is a promising target for the development of novel antimalarial drugs. Here, the crystal structure of the truncated zymogen of PM IV (pPM IV), consisting of the mature enzyme plus a prosegment of 47 residues, has been determined at 1.5 A resolution. pPM IV presents the fold previously described for studied proplasmepsins, displaying closer similarities to proplasmepin IV from P. vivax (pPvPM) than to the other two proplasmepsins from P. falciparum. The study and comparison of the pPM IV structure with the proplasmepsin structures described previously provide information about the similarities and differences in the inactivation-activation mechanisms among the plasmepsin zymogens. | ||
| - | + | Crystal structure of Plasmodium falciparum proplasmepsin IV: the plasticity of proplasmepsins.,Recacha R, Jaudzems K, Akopjana I, Jirgensons A, Tars K Acta Crystallogr F Struct Biol Commun. 2016 Sep;72(Pt 9):659-66. doi:, 10.1107/S2053230X16011663. Epub 2016 Aug 9. PMID:27599854<ref>PMID:27599854</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5bwy" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| - | [[Category: | + | ==See Also== |
| - | [[Category: Recacha | + | *[[Plasmepsin|Plasmepsin]] |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Plasmodium falciparum]] | ||
| + | [[Category: Akopjana I]] | ||
| + | [[Category: Jaudzems K]] | ||
| + | [[Category: Recacha R]] | ||
| + | [[Category: Tars K]] | ||
Current revision
Structure of proplasmepsin II from Plasmodium falciparum, Space Group P43212
| |||||||||||
