8wxw
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Falcilysin in complex with hemoglobin alpha chain peptide== | |
| - | + | <StructureSection load='8wxw' size='340' side='right'caption='[[8wxw]], [[Resolution|resolution]] 1.86Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8wxw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8WXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WXW 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]] 1.86Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=8wxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wxw OCA], [https://pdbe.org/8wxw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wxw RCSB], [https://www.ebi.ac.uk/pdbsum/8wxw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wxw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FCLN_PLAF7 FCLN_PLAF7] In the food vacuole, acts downstream of proteases plasmepsins PMI and PMII and falcipains during the catabolism of host hemoglobin by cleaving peptide fragments of alpha and beta hemoglobin subunits generated by PMI and PMII and falcipains (PubMed:17074076). In the apicoplast, degrades apicoplast transit peptides after their cleavage (PubMed:17074076). Prefers bulky hydrophobic amino acids in the P1' position at both acidic and neutral pH (By similarity). At P2', prefers hydrophobic residues at acidic pH; at neutral pH, these same residues are abundant but prefers Arg (By similarity). At P3', prefers hydrophobic residues, especially Met, at both pH conditions. At P4' and P5', prefers acidic residues at acidic pH, however, at neutral pH, the enzyme is less selective at these positions (By similarity). The optimal site cleavage at acidic pH is YNEHS-|-FFMEE and, at neutral pH, MKRHS-|-FRMRG (By similarity).[UniProtKB:A0A0L7KF24]<ref>PMID:17074076</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Plasmodium falciparum 3D7]] | ||
| + | [[Category: Lescar J]] | ||
| + | [[Category: Lin JQ]] | ||
Current revision
Falcilysin in complex with hemoglobin alpha chain peptide
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