1pfz
From Proteopedia
(Difference between revisions)
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<StructureSection load='1pfz' size='340' side='right'caption='[[1pfz]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='1pfz' size='340' side='right'caption='[[1pfz]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1pfz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1pfz]] is a 4 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=1PFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PFZ FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=1pfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pfz OCA], [https://pdbe.org/1pfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pfz RCSB], [https://www.ebi.ac.uk/pdbsum/1pfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pfz ProSAT]</span></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=1pfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pfz OCA], [https://pdbe.org/1pfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pfz RCSB], [https://www.ebi.ac.uk/pdbsum/1pfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pfz ProSAT]</span></td></tr> | ||
</table> | </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:8844673, PubMed:11782538, PubMed:15574427). 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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1pfz ConSurf]. | </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=1pfz ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Proplasmepsin II is the zymogen of plasmepsin II, an aspartic proteinase used by Plasmodiumfalciparum to digest hemoglobin during the blood stage of malaria. A large shift between the N-domain and the central and C-domains of proplasmepsin II opens the active site cleft, preventing the formation of a functional aspartic proteinase active site. This mode of inhibition of catalytic activity has not been observed in any other aspartic proteinase zymogen. Instead of occluding a pre-formed active site, as in the gastric aspartic proteinase zymogens, the prosegment of proplasmepsin II interacts extensively with the C-domain and serves as a 'harness' to keep the domains apart. Disruption of key salt bridges at low pH may be important in activation. | ||
- | |||
- | Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from plasmodium falciparum.,Bernstein NK, Cherney MM, Loetscher H, Ridley RG, James MN Nat Struct Biol. 1999 Jan;6(1):32-7. PMID:9886289<ref>PMID:9886289</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1pfz" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Plasmodium falciparum]] |
- | + | [[Category: Bernstein NK]] | |
- | [[Category: Bernstein | + | [[Category: Cherney MM]] |
- | [[Category: Cherney | + | [[Category: James MNG]] |
- | [[Category: James | + | [[Category: Loetscher H]] |
- | [[Category: Loetscher | + | [[Category: Ridley RG]] |
- | [[Category: Ridley | + | |
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Revision as of 05:55, 17 April 2024
PROPLASMEPSIN II FROM PLASMODIUM FALCIPARUM
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