1w6h: Difference between revisions

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<StructureSection load='1w6h' size='340' side='right'caption='[[1w6h]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
<StructureSection load='1w6h' size='340' side='right'caption='[[1w6h]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1w6h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plafa Plafa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W6H FirstGlance]. <br>
<table><tr><td colspan='2'>[[1w6h]] is a 2 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=1W6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W6H FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TIT:N-((3S,4S)-5-[(4-BROMOBENZYL)OXY]-3-HYDROXY-4-{[N-(PYRIDIN-2-YLCARBONYL)-L-VALYL]AMINO}PENTANOYL)-L-ALANYL-L-LEUCINAMIDE'>TIT</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]] 2.24&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1j8j|1j8j]], [[1lee|1lee]], [[1lf2|1lf2]], [[1lf3|1lf3]], [[1lf4|1lf4]], [[1m43|1m43]], [[1me6|1me6]], [[1pfz|1pfz]], [[1sme|1sme]], [[1w6i|1w6i]], [[1xdh|1xdh]], [[1xe5|1xe5]], [[1xe6|1xe6]], [[2bju|2bju]], [[2bl3|2bl3]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TIT:N-((3S,4S)-5-[(4-BROMOBENZYL)OXY]-3-HYDROXY-4-{[N-(PYRIDIN-2-YLCARBONYL)-L-VALYL]AMINO}PENTANOYL)-L-ALANYL-L-LEUCINAMIDE'>TIT</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Plasmepsin_II Plasmepsin II], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.39 3.4.23.39] </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=1w6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w6h OCA], [https://pdbe.org/1w6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w6h RCSB], [https://www.ebi.ac.uk/pdbsum/1w6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w6h 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=1w6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w6h OCA], [https://pdbe.org/1w6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w6h RCSB], [https://www.ebi.ac.uk/pdbsum/1w6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w6h 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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==See Also==
==See Also==
*[[Plasmepsin|Plasmepsin]]
*[[Plasmepsin|Plasmepsin]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Plafa]]
[[Category: Plasmodium falciparum]]
[[Category: Plasmepsin II]]
[[Category: Johansson P-O]]
[[Category: Johansson, P O]]
[[Category: Kvarnstroem I]]
[[Category: Kvarnstroem, I]]
[[Category: Lindberg J]]
[[Category: Lindberg, J]]
[[Category: Rosenquist A]]
[[Category: Rosenquist, A]]
[[Category: Samuelsson B]]
[[Category: Samuelsson, B]]
[[Category: Unge T]]
[[Category: Unge, T]]
[[Category: Vrang L]]
[[Category: Vrang, L]]
[[Category: Aspartic protease]]
[[Category: Drug]]
[[Category: Glycoprotein]]
[[Category: Hydrolase]]
[[Category: Malaria]]
[[Category: Plasmepsin]]

Revision as of 16:31, 9 May 2024

Novel plasmepsin II-inhibitor complexNovel plasmepsin II-inhibitor complex

Structural highlights

1w6h is a 2 chain structure with sequence from Plasmodium falciparum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.24Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Banerjee R, Liu J, Beatty W, Pelosof L, Klemba M, Goldberg DE. Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine. Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):990-5. doi: 10.1073/pnas.022630099., Epub 2002 Jan 8. PMID:11782538 doi:http://dx.doi.org/10.1073/pnas.022630099
  2. ↑ Istvan ES, Goldberg DE. Distal substrate interactions enhance plasmepsin activity. J Biol Chem. 2005 Feb 25;280(8):6890-6. doi: 10.1074/jbc.M412086200. Epub 2004, Dec 1. PMID:15574427 doi:http://dx.doi.org/10.1074/jbc.M412086200
  3. ↑ Luker KE, Francis SE, Gluzman IY, Goldberg DE. Kinetic analysis of plasmepsins I and II aspartic proteases of the Plasmodium falciparum digestive vacuole. Mol Biochem Parasitol. 1996 Jul;79(1):71-8. doi: 10.1016/0166-6851(96)02651-5. PMID:8844673 doi:http://dx.doi.org/10.1016/0166-6851(96)02651-5

1w6h, resolution 2.24Å

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