4x2t

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<StructureSection load='4x2t' size='340' side='right'caption='[[4x2t]], [[Resolution|resolution]] 2.73&Aring;' scene=''>
<StructureSection load='4x2t' size='340' side='right'caption='[[4x2t]], [[Resolution|resolution]] 2.73&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4x2t]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Plaf7 Plaf7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X2T FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4x2t]] is a 12 chain structure with sequence from [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=4X2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X2T FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TOD:(2S)-({(2R)-2-[(1S)-1-HYDROXY-2-(HYDROXYAMINO)-2-OXOETHYL]-4-METHYLPENTANOYL}AMINO)(PHENYL)ETHANOIC+ACID'>TOD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.729&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kqx|3kqx]], [[3kqz|3kqz]], [[3kr4|3kr4]], [[4x2u|4x2u]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TOD:(2S)-({(2R)-2-[(1S)-1-HYDROXY-2-(HYDROXYAMINO)-2-OXOETHYL]-4-METHYLPENTANOYL}AMINO)(PHENYL)ETHANOIC+ACID'>TOD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LAP, PF14_0439 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4x2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x2t OCA], [https://pdbe.org/4x2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x2t RCSB], [https://www.ebi.ac.uk/pdbsum/4x2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x2t ProSAT]</span></td></tr>
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<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=4x2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x2t OCA], [http://pdbe.org/4x2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x2t RCSB], [http://www.ebi.ac.uk/pdbsum/4x2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x2t ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMPL_PLAF7 AMPL_PLAF7] Aminopeptidase which preferentially cleaves leucine residues from the N-terminus of peptides (PubMed:17107951, PubMed:21844374, PubMed:22359643, PubMed:33536500, PubMed:34133730). Also, has some activity towards tryptophan and methionine and to a lesser extent towards phenylalanine (PubMed:17107951, PubMed:22359643, PubMed:34133730). Has very low activity or no activity towards the other amino acids (PubMed:17107951, PubMed:22359643, PubMed:34133730). In addition, cleaves the Cys-Gly dipeptide, probably as part of the glutathione regulation pathway; cleavage only occurs in the presence of Mn(2+) (PubMed:33303633). During the asexual blood stage, plays a role in the final step of host hemoglobin catabolism, by cleaving hemoglobin-derived oligopeptides providing a source of amino acids for the parasite protein synthesis and for the maintenance of osmotic homeostasis (PubMed:34133730). During the asexual blood stage, may also play a role during the ring-trophozoite transition (PubMed:21844374).<ref>PMID:17107951</ref> <ref>PMID:21844374</ref> <ref>PMID:22359643</ref> <ref>PMID:33303633</ref> <ref>PMID:33536500</ref> <ref>PMID:34133730</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Plaf7]]
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[[Category: Plasmodium falciparum 3D7]]
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[[Category: Drinkwater, N]]
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[[Category: Drinkwater N]]
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[[Category: McGowan, S]]
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[[Category: McGowan S]]
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[[Category: Antimalarial]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Inhibitor]]
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[[Category: M17 leucyl-aminopeptidase]]
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[[Category: Plasmodium falciparum]]
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[[Category: Protease]]
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[[Category: Tosedostat]]
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Current revision

X-ray crystal structure of the orally available aminopeptidase inhibitor, Tosedostat, bound to the M17 Leucyl Aminopeptidase from P. falciparum

PDB ID 4x2t

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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