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| | <StructureSection load='4lvn' size='340' side='right'caption='[[4lvn]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='4lvn' size='340' side='right'caption='[[4lvn]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4lvn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Plafa Plafa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LVN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LVN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4lvn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LVN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sub-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 PLAFA])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Kexin Kexin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.61 3.4.21.61] </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=4lvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lvn OCA], [https://pdbe.org/4lvn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lvn RCSB], [https://www.ebi.ac.uk/pdbsum/4lvn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lvn ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lvn OCA], [http://pdbe.org/4lvn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lvn RCSB], [http://www.ebi.ac.uk/pdbsum/4lvn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lvn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SUB1_PLAFA SUB1_PLAFA] Serine protease which plays an essential role in merozoite invasion of and egress from host erythrocytes by processing and activating various merozoite surface and parasitophorous vacuole proteins. Mediates the proteolytic maturation of serine proteases SERA4, SERA5 and SERA6 just prior to merozoite egress. Prior to merozoite egress, cleaves merozoite surface proteins MSP1, MSP6 and MSP7, which form the MSP1/6/7 complex, and thereby may prime the parasite cell surface for invasion of fresh erythrocytes. Prior to merozoite egress, cleaves MSRP2 converting it to MSRP2 p25 form, and RAP1 converting it to RAP1 p67 form.[UniProtKB:Q8I0V0] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Kexin]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Plafa]] | + | [[Category: Plasmodium falciparum]] |
| - | [[Category: Blackman, M J]] | + | [[Category: Blackman MJ]] |
| - | [[Category: Withers-Martinez, C]] | + | [[Category: Withers-Martinez C]] |
| - | [[Category: Alpha beta]]
| + | |
| - | [[Category: Calcium ion]]
| + | |
| - | [[Category: Enzyme-prodomain complex]]
| + | |
| - | [[Category: Hydrolase-inhibitor-immune system complex]]
| + | |
| - | [[Category: Parasitophorous vacuole]]
| + | |
| - | [[Category: Prodomain]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Serine protease]]
| + | |
| Structural highlights
Function
SUB1_PLAFA Serine protease which plays an essential role in merozoite invasion of and egress from host erythrocytes by processing and activating various merozoite surface and parasitophorous vacuole proteins. Mediates the proteolytic maturation of serine proteases SERA4, SERA5 and SERA6 just prior to merozoite egress. Prior to merozoite egress, cleaves merozoite surface proteins MSP1, MSP6 and MSP7, which form the MSP1/6/7 complex, and thereby may prime the parasite cell surface for invasion of fresh erythrocytes. Prior to merozoite egress, cleaves MSRP2 converting it to MSRP2 p25 form, and RAP1 converting it to RAP1 p67 form.[UniProtKB:Q8I0V0]
Publication Abstract from PubMed
Malaria is caused by a protozoan parasite that replicates within an intraerythrocytic parasitophorous vacuole. Release (egress) of malaria merozoites from the host erythrocyte is a highly regulated and calcium-dependent event that is critical for disease progression. Minutes before egress, an essential parasite serine protease called SUB1 is discharged into the parasitophorous vacuole, where it proteolytically processes a subset of parasite proteins that play indispensable roles in egress and invasion. Here we report the first crystallographic structure of Plasmodium falciparum SUB1 at 2.25 A, in complex with its cognate prodomain. The structure highlights the basis of the calcium dependence of SUB1, as well as its unusual requirement for interactions with substrate residues on both prime and non-prime sides of the scissile bond. Importantly, the structure also reveals the presence of a solvent-exposed redox-sensitive disulphide bridge, unique among the subtilisin family, that likely acts as a regulator of protease activity in the parasite.
The malaria parasite egress protease SUB1 is a calcium-dependent redox switch subtilisin.,Withers-Martinez C, Strath M, Hackett F, Haire LF, Howell SA, Walker PA, Evangelos C, Dodson GG, Blackman MJ Nat Commun. 2014 May 2;5:3726. doi: 10.1038/ncomms4726. PMID:24785947[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Withers-Martinez C, Strath M, Hackett F, Haire LF, Howell SA, Walker PA, Evangelos C, Dodson GG, Blackman MJ. The malaria parasite egress protease SUB1 is a calcium-dependent redox switch subtilisin. Nat Commun. 2014 May 2;5:3726. doi: 10.1038/ncomms4726. PMID:24785947 doi:http://dx.doi.org/10.1038/ncomms4726
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