7vpe
From Proteopedia
(Difference between revisions)
| (One intermediate revision not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Falcilysin in complex with A1== | |
| - | + | <StructureSection load='7vpe' size='340' side='right'caption='[[7vpe]], [[Resolution|resolution]] 1.62Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[7vpe]] 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=7VPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VPE 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]] 1.62Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7TU:(4S,5S)-1-[[3-[[(4S,5S)-4,5-diphenyl-4,5-dihydroimidazol-1-yl]methyl]phenyl]methyl]-4,5-diphenyl-4,5-dihydroimidazole'>7TU</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=7vpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vpe OCA], [https://pdbe.org/7vpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vpe RCSB], [https://www.ebi.ac.uk/pdbsum/7vpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vpe 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: Large Structures]] | ||
| + | [[Category: Plasmodium falciparum]] | ||
| + | [[Category: El Sahili A]] | ||
| + | [[Category: Lescar J]] | ||
| + | [[Category: Lin JQ]] | ||
Current revision
Falcilysin in complex with A1
| |||||||||||
