3ch3

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(New page: 200px {{Structure |PDB= 3ch3 |SIZE=350|CAPTION= <scene name='initialview01'>3ch3</scene>, resolution 1.79&Aring; |SITE= <scene name='pdbsite=AC1:K+Binding+Site+Fo...)
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[[Image:3ch3.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure Analysis of SERA5E from plasmodium falciparum==
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|PDB= 3ch3 |SIZE=350|CAPTION= <scene name='initialview01'>3ch3</scene>, resolution 1.79&Aring;
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<StructureSection load='3ch3' size='340' side='right'caption='[[3ch3]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:K+Binding+Site+For+Residue+X+1'>AC1</scene>, <scene name='pdbsite=AC2:2hp+Binding+Site+For+Residue+X+829'>AC2</scene> and <scene name='pdbsite=AC3:2hp+Binding+Site+For+Residue+X+830'>AC3</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=2HP:DIHYDROGENPHOSPHATE+ION'>2HP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>
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<table><tr><td colspan='2'>[[3ch3]] is a 1 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=3CH3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CH3 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]] 1.79&#8491;</td></tr>
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|GENE= SERA5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 Plasmodium falciparum])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2HP:DIHYDROGENPHOSPHATE+ION'>2HP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd02619 Peptidase_C1]</span>
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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=3ch3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ch3 OCA], [https://pdbe.org/3ch3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ch3 RCSB], [https://www.ebi.ac.uk/pdbsum/3ch3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ch3 ProSAT]</span></td></tr>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ch3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ch3 OCA], [http://www.ebi.ac.uk/pdbsum/3ch3 PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=3ch3 RCSB]</span>
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</table>
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}}
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== Function ==
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[https://www.uniprot.org/uniprot/SERA5_PLAF7 SERA5_PLAF7] Plays an essential role during the asexual blood stage development by controlling the kinetics of merozoite egress from host erythrocytes (PubMed:25599609, PubMed:28683142). Specifically, prevents premature rupture of the parasitophorous vacuole and host erythrocyte membranes (PubMed:28683142).<ref>PMID:25599609</ref> <ref>PMID:28683142</ref> May prevent merozoite phagocytosis by host monocytes via interaction with host VTN at the merozoite surface (By similarity). Plays a role in parasite growth (By similarity).[UniProtKB:P69193] Protease activity is controversial (PubMed:25599609). Has been shown in a number of studies to have protease activity towards a synthetic peptide in vitro (PubMed:13679369, PubMed:24769454, PubMed:29716996). Has also been shown to lack protease activity towards a synthetic peptide in vitro (PubMed:25599609).<ref>PMID:13679369</ref> <ref>PMID:24769454</ref> <ref>PMID:25599609</ref> <ref>PMID:29716996</ref>
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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/ch/3ch3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3ch3 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The sera genes of the malaria-causing parasite Plasmodium encode a family of unique proteins that are maximally expressed at the time of egress of parasites from infected red blood cells. These multi-domain proteins are unique, containing a central papain-like cysteine-protease fragment enclosed between the disulfide-linked N- and C-terminal domains. However, the central fragment of several members of this family, including serine repeat antigen 5 (SERA5), contains a serine (S596) in place of the active-site cysteine. Here we report the crystal structure of the central protease-like domain of Plasmodium falciparum SERA5, revealing a number of anomalies in addition to the putative nucleophilic serine: (1) the structure of the putative active site is not conducive to binding substrate in the canonical cysteine-protease manner; (2) the side chain of D594 restricts access of substrate to the putative active site; and (3) the S(2) specificity pocket is occupied by the side chain of Y735, reducing this site to a small depression on the protein surface. Attempts to determine the structure in complex with known inhibitors were not successful. Thus, despite having revealed its structure, the function of the catalytic domain of SERA5 remains an enigma.
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'''Crystal Structure Analysis of SERA5E from plasmodium falciparum'''
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Structural insights into the protease-like antigen Plasmodium falciparum SERA5 and its noncanonical active-site serine.,Hodder AN, Malby RL, Clarke OB, Fairlie WD, Colman PM, Crabb BS, Smith BJ J Mol Biol. 2009 Sep 11;392(1):154-65. Epub 2009 Jul 8. PMID:19591843<ref>PMID:19591843</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==About this Structure==
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</div>
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3CH3 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=3CH3 OCA].
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<div class="pdbe-citations 3ch3" style="background-color:#fffaf0;"></div>
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[[Category: Plasmodium falciparum]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Clarke, O B.]]
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__TOC__
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[[Category: Colman, P M.]]
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</StructureSection>
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[[Category: Malby, R L.]]
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[[Category: Large Structures]]
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[[Category: Smith, B J.]]
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[[Category: Plasmodium falciparum 3D7]]
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[[Category: cysteine protease]]
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[[Category: Clarke OB]]
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[[Category: glycoprotein]]
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[[Category: Colman PM]]
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[[Category: hydrolase]]
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[[Category: Malby RL]]
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[[Category: malaria]]
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[[Category: Smith BJ]]
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[[Category: papain family]]
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[[Category: thiol protease]]
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[[Category: vacuole]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 09:59:14 2008''
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Current revision

Crystal Structure Analysis of SERA5E from plasmodium falciparum

PDB ID 3ch3

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