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[[Image:1m43.gif|left|200px]]


{{Structure
==Crystal structure of PMII in complex with pepstatin a to 2.4 A==
|PDB= 1m43 |SIZE=350|CAPTION= <scene name='initialview01'>1m43</scene>, resolution 2.40&Aring;
<StructureSection load='1m43' size='340' side='right'caption='[[1m43]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=IHN:3-HYDROXY-4-ISOBUTYL-4-[AMINOCARBONYLETHYL(AMINO+CARBONYL-2-HYDROXY-5-METHYLHEXYL)TRI(AMINOCARBONYL+ISOBUTYL)]BUTANOIC+ACID'>IHN</scene>
<table><tr><td colspan='2'>[[1m43]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] and [https://en.wikipedia.org/wiki/Streptomyces_argenteolus_subsp._toyonakensis Streptomyces argenteolus subsp. toyonakensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M43 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M43 FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Plasmepsin_II Plasmepsin II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.39 3.4.23.39] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IVA:ISOVALERIC+ACID'>IVA</scene>, <scene name='pdbligand=STA:STATINE'>STA</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m43 OCA], [https://pdbe.org/1m43 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m43 RCSB], [https://www.ebi.ac.uk/pdbsum/1m43 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m43 ProSAT]</span></td></tr>
|RELATEDENTRY=[[1sme|1SME]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m43 OCA], [http://www.ebi.ac.uk/pdbsum/1m43 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m43 RCSB]</span>
== 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:11782538, PubMed:15574427, PubMed:8844673). 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m4/1m43_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m43 ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF PMII IN COMPLEX WITH PEPSTATIN A TO 2.4 A'''
==See Also==
 
*[[Plasmepsin|Plasmepsin]]
 
== References ==
==About this Structure==
<references/>
1M43 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M43 OCA].
__TOC__
[[Category: Plasmepsin II]]
</StructureSection>
[[Category: Large Structures]]
[[Category: Plasmodium falciparum]]
[[Category: Plasmodium falciparum]]
[[Category: Single protein]]
[[Category: Streptomyces argenteolus subsp. toyonakensis]]
[[Category: Asojo, O A.]]
[[Category: Asojo OA]]
[[Category: Gulnik, S.]]
[[Category: Gulnik S]]
[[Category: Silva, A M.]]
[[Category: Silva AM]]
[[Category: plasmepsin ii]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:10:55 2008''

Latest revision as of 10:00, 30 October 2024

Crystal structure of PMII in complex with pepstatin a to 2.4 ACrystal structure of PMII in complex with pepstatin a to 2.4 A

Structural highlights

1m43 is a 4 chain structure with sequence from Plasmodium falciparum and Streptomyces argenteolus subsp. toyonakensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
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:11782538, PubMed:15574427, PubMed:8844673). 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

1m43, resolution 2.40Å

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