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| | ==Crystal structure of Cryptosporidium parvum pyruvate kinase== | | ==Crystal structure of Cryptosporidium parvum pyruvate kinase== |
| - | <StructureSection load='4drs' size='340' side='right' caption='[[4drs]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='4drs' size='340' side='right'caption='[[4drs]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4drs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cryptosporidium_parvum_iowa_ii Cryptosporidium parvum iowa ii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DRS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DRS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4drs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryptosporidium_parvum_Iowa_II Cryptosporidium parvum Iowa II]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DRS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DRS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cgd1_2040 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=353152 Cryptosporidium parvum Iowa II])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] </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=4drs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4drs OCA], [https://pdbe.org/4drs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4drs RCSB], [https://www.ebi.ac.uk/pdbsum/4drs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4drs ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4drs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4drs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4drs RCSB], [http://www.ebi.ac.uk/pdbsum/4drs PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5CSM7_CRYPI Q5CSM7_CRYPI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4drs" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Pyruvate Kinase|Pyruvate Kinase]] | + | *[[Pyruvate kinase 3D structures|Pyruvate kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cryptosporidium parvum iowa ii]] | + | [[Category: Cryptosporidium parvum Iowa II]] |
| - | [[Category: Pyruvate kinase]] | + | [[Category: Large Structures]] |
| - | [[Category: Chattopadhyay, D]] | + | [[Category: Chattopadhyay D]] |
| - | [[Category: Cook, W J]] | + | [[Category: Cook WJ]] |
| - | [[Category: Allosteric enzyme]]
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| - | [[Category: Cryptosporidium]]
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| - | [[Category: Glycolysis]]
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| - | [[Category: Kinase]]
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| - | [[Category: Pyruvate]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
Q5CSM7_CRYPI
Publication Abstract from PubMed
Pyruvate kinase plays a critical role in cellular metabolism of glucose by serving as a major regulator of glycolysis. This tetrameric enzyme is allosterically regulated by different effector molecules, mainly phosphosugars. In response to binding of effector molecules and substrates, significant structural changes have been identified in various pyruvate kinase structures. Pyruvate kinase of Cryptosporidium parvum is exceptional among known enzymes of protozoan origin in that it exhibits no allosteric property in the presence of commonly known effector molecules. The crystal structure of pyruvate kinase from C. parvum has been solved by molecular replacement techniques and refined to 2.5 A resolution. In the active site a glycerol molecule is located near the gamma-phosphate site of ATP, and the protein structure displays a partially closed active site. However, unlike other structures where the active site is closed, the alpha6' helix in C. parvum pyruvate kinase unwinds and assumes an extended conformation. In the crystal structure a sulfate ion is found at a site that is occupied by a phosphate of the effector molecule in many pyruvate kinase structures. A new feature of the C. parvum pyruvate kinase structure is the presence of a disulfide bond cross-linking the two monomers in the asymmetric unit. The disulfide bond is formed between cysteine residue 26 in the short N-helix of one monomer with cysteine residue 312 in a long helix (residues 303-320) of the second monomer at the interface of these monomers. Both cysteine residues are unique to C. parvum, and the disulfide bond remained intact in a reduced environment. However, the significance of this bond, if any, remains unknown at this time.
Crystal structure of Cryptosporidium parvum pyruvate kinase.,Cook WJ, Senkovich O, Aleem K, Chattopadhyay D PLoS One. 2012;7(10):e46875. doi: 10.1371/journal.pone.0046875. Epub 2012 Oct 9. PMID:23056503[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cook WJ, Senkovich O, Aleem K, Chattopadhyay D. Crystal structure of Cryptosporidium parvum pyruvate kinase. PLoS One. 2012;7(10):e46875. doi: 10.1371/journal.pone.0046875. Epub 2012 Oct 9. PMID:23056503 doi:http://dx.doi.org/10.1371/journal.pone.0046875
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