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1miq

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[[Image:1miq.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of proplasmepsin from the human malarial pathogen Plasmodium vivax==
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|PDB= 1miq |SIZE=350|CAPTION= <scene name='initialview01'>1miq</scene>, resolution 2.5&Aring;
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<StructureSection load='1miq' size='340' side='right'caption='[[1miq]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1miq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_vivax Plasmodium vivax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MIQ FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.5&#8491;</td></tr>
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|GENE=
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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=1miq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1miq OCA], [https://pdbe.org/1miq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1miq RCSB], [https://www.ebi.ac.uk/pdbsum/1miq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1miq ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1qs8|1qs8]], [[1pfz|1pfz]], [[1ls5|1ls5]], [[1sme|1sme]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1miq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1miq OCA], [http://www.ebi.ac.uk/pdbsum/1miq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1miq RCSB]</span>
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[https://www.uniprot.org/uniprot/O60989_PLAVI O60989_PLAVI]
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mi/1miq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1miq ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of proplasmepsin from the human malarial pathogen Plasmodium vivax'''
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==See Also==
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*[[Plasmepsin|Plasmepsin]]
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__TOC__
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==Overview==
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</StructureSection>
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The malarial aspartic proteinases (plasmepsins) have been discovered in several species of Plasmodium, including all four of the human malarial pathogens. In P.falciparum, plasmepsins I, II, IV and HAP have been directly implicated in hemoglobin degradation during malaria infection, and are now considered targets for anti-malarial drug design. The plasmepsins are produced from inactive zymogens, proplasmepsins, having unusually long N-terminal prosegments of more than 120 amino acids. Structural and biochemical evidence suggests that the conversion process of proplasmepsins to plasmepsins differs substantially from the gastric and plant aspartic proteinases. Instead of blocking substrate access to a pre-formed active site, the prosegment enforces a conformation in which proplasmepsin cannot form a functional active site. We have determined crystal structures of plasmepsin and proplasmepsin from P.vivax. The three-dimensional structure of P.vivax plasmepsin is typical of the monomeric aspartic proteinases, and the structure of P.vivax proplasmepsin is similar to that of P.falciparum proplasmepsin II. A dramatic refolding of the mature N terminus and a large (18 degrees ) reorientation of the N-domain between P.vivax proplasmepsin and plasmepsin results in a severe distortion of the active site region of the zymogen relative to that of the mature enzyme. The present structures confirm that the mode of inactivation observed originally in P.falciparum proplasmepsin II, i.e. an incompletely formed active site, is a true structural feature and likely represents the general mode of inactivation of the related proplasmepsins.
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[[Category: Large Structures]]
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==About this Structure==
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1MIQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_vivax Plasmodium vivax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MIQ OCA].
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==Reference==
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Structural insights into the activation of P. vivax plasmepsin., Bernstein NK, Cherney MM, Yowell CA, Dame JB, James MN, J Mol Biol. 2003 Jun 6;329(3):505-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12767832 12767832]
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[[Category: Plasmodium vivax]]
[[Category: Plasmodium vivax]]
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[[Category: Single protein]]
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[[Category: Bernstein NK]]
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[[Category: Bernstein, N K.]]
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[[Category: Cherney MM]]
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[[Category: Cherney, M M.]]
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[[Category: Dame JB]]
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[[Category: Dame, J B.]]
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[[Category: James MN]]
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[[Category: James, M N.]]
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[[Category: Yowell CA]]
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[[Category: Yowell, C A.]]
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[[Category: aspartic proteinase zymogen]]
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[[Category: domain opening]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:16:38 2008''
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Current revision

Crystal structure of proplasmepsin from the human malarial pathogen Plasmodium vivax

PDB ID 1miq

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