3eoz: Difference between revisions
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< | ==Crystal Structure of Phosphoglycerate Mutase from Plasmodium Falciparum, PFD0660w== | ||
<StructureSection load='3eoz' size='340' side='right'caption='[[3eoz]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3eoz]] is a 2 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=3EOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EOZ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=3eoz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eoz OCA], [https://pdbe.org/3eoz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eoz RCSB], [https://www.ebi.ac.uk/pdbsum/3eoz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eoz ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8I1V2_PLAF7 Q8I1V2_PLAF7] | |||
== 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/eo/3eoz_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=3eoz ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Plasmodium falciparum malaria is the most important parasitic disease worldwide, responsible for an estimated 1 million deaths annually. Two P. falciparum genes code for putative phosphoglycerate mutases (PGMases), a widespread protein group characterized by the involvement of histidine residues in their catalytic mechanism. PGMases are responsible for the interconversion between 2 and 3-phosphoglycerate, an intermediate step in the glycolysis pathway. We have determined the crystal structures of one of the P. falciparum's PGMases (PfPGM2) and a functionally distinct phosphoglycerate mutase from Cryptosporidium parvum, a related apicomplexan parasite. We performed sequence and structural comparisons between the two structures, another P. falciparum enzyme (PfPGM1) and several other PGM family members from other organisms. The comparisons revealed a distinct conformation of the catalytically active residues not seen in previously determined phosphoglycerate mutase structures. Furthermore, characterization of their enzymatic activities revealed contrasting behaviors between the PfPGM2 and the classical cofactor-dependent PGMase from C. parvum, clearly establishing PfPGM2 as a phosphatase with a residual level of mutase activity. Further support for this function attribution was provided by our structural comparison with previously characterized PGM family members. Genetic characterization of PGM2 in the rodent parasite Plasmodium berghei indicated that the protein might be essential to blood stage asexual growth, and a GFP tagged allele is expressed in both blood and zygote ookinete development and located in the cytoplasm. The P. falciparum PGM2 is either an enzyme implicated in the phosphate metabolism of the parasite or a regulator of its life cycle. | |||
Characterization of a new phosphatase from Plasmodium.,Hills T, Srivastava A, Ayi K, Wernimont AK, Kain K, Waters AP, Hui R, Pizarro JC Mol Biochem Parasitol. 2011 Oct;179(2):69-79. Epub 2011 Jun 13. PMID:21689687<ref>PMID:21689687</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3eoz" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: Plasmodium falciparum 3D7]] | |||
[[Category: Arrowsmith CH]] | |||
== | [[Category: Bochkarev A]] | ||
< | [[Category: Cossar D]] | ||
[[Category: | [[Category: Edwards AM]] | ||
[[Category: Plasmodium falciparum]] | [[Category: Hills T]] | ||
[[Category: Arrowsmith | [[Category: Hui R]] | ||
[[Category: Bochkarev | [[Category: Kozieradzki I]] | ||
[[Category: Cossar | [[Category: Lam A]] | ||
[[Category: Edwards | [[Category: Lew J]] | ||
[[Category: Hills | [[Category: Lin YH]] | ||
[[Category: Hui | [[Category: Pizarro J]] | ||
[[Category: Kozieradzki | [[Category: Schapira M]] | ||
[[Category: Lam | [[Category: Tempel W]] | ||
[[Category: Lew | [[Category: Vedadi M]] | ||
[[Category: Lin | [[Category: Wasney G]] | ||
[[Category: Pizarro | [[Category: Weigelt J]] | ||
[[Category: Wernimont AK]] | |||
[[Category: Schapira | [[Category: Zhao Y]] | ||
[[Category: Tempel | |||
[[Category: Vedadi | |||
[[Category: Wasney | |||
[[Category: Weigelt | |||
[[Category: Wernimont | |||
[[Category: Zhao | |||
Latest revision as of 12:50, 6 November 2024
Crystal Structure of Phosphoglycerate Mutase from Plasmodium Falciparum, PFD0660wCrystal Structure of Phosphoglycerate Mutase from Plasmodium Falciparum, PFD0660w
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPlasmodium falciparum malaria is the most important parasitic disease worldwide, responsible for an estimated 1 million deaths annually. Two P. falciparum genes code for putative phosphoglycerate mutases (PGMases), a widespread protein group characterized by the involvement of histidine residues in their catalytic mechanism. PGMases are responsible for the interconversion between 2 and 3-phosphoglycerate, an intermediate step in the glycolysis pathway. We have determined the crystal structures of one of the P. falciparum's PGMases (PfPGM2) and a functionally distinct phosphoglycerate mutase from Cryptosporidium parvum, a related apicomplexan parasite. We performed sequence and structural comparisons between the two structures, another P. falciparum enzyme (PfPGM1) and several other PGM family members from other organisms. The comparisons revealed a distinct conformation of the catalytically active residues not seen in previously determined phosphoglycerate mutase structures. Furthermore, characterization of their enzymatic activities revealed contrasting behaviors between the PfPGM2 and the classical cofactor-dependent PGMase from C. parvum, clearly establishing PfPGM2 as a phosphatase with a residual level of mutase activity. Further support for this function attribution was provided by our structural comparison with previously characterized PGM family members. Genetic characterization of PGM2 in the rodent parasite Plasmodium berghei indicated that the protein might be essential to blood stage asexual growth, and a GFP tagged allele is expressed in both blood and zygote ookinete development and located in the cytoplasm. The P. falciparum PGM2 is either an enzyme implicated in the phosphate metabolism of the parasite or a regulator of its life cycle. Characterization of a new phosphatase from Plasmodium.,Hills T, Srivastava A, Ayi K, Wernimont AK, Kain K, Waters AP, Hui R, Pizarro JC Mol Biochem Parasitol. 2011 Oct;179(2):69-79. Epub 2011 Jun 13. PMID:21689687[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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