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| | <StructureSection load='5azj' size='340' side='right'caption='[[5azj]], [[Resolution|resolution]] 2.61Å' scene=''> | | <StructureSection load='5azj' size='340' side='right'caption='[[5azj]], [[Resolution|resolution]] 2.61Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5azj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Trybg Trybg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AZJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AZJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5azj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_gambiense Trypanosoma brucei gambiense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AZJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AZJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4NP:4-NITROPHENYL+PHOSPHATE'>4NP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4NP:4-NITROPHENYL+PHOSPHATE'>4NP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=5azj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5azj OCA], [https://pdbe.org/5azj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5azj RCSB], [https://www.ebi.ac.uk/pdbsum/5azj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5azj ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5azi|5azi]]</td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=31285 TRYBG])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycerol_kinase Glycerol kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.30 2.7.1.30] </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=5azj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5azj OCA], [http://pdbe.org/5azj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5azj RCSB], [http://www.ebi.ac.uk/pdbsum/5azj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5azj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/D3KVM3_TRYBG D3KVM3_TRYBG] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glycerol kinase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Trybg]] | + | [[Category: Trypanosoma brucei gambiense]] |
| - | [[Category: Balogun, E O]] | + | [[Category: Balogun EO]] |
| - | [[Category: Harada, S]] | + | [[Category: Harada S]] |
| - | [[Category: Inaoka, D K]] | + | [[Category: Inaoka DK]] |
| - | [[Category: Kita, K]] | + | [[Category: Kita K]] |
| - | [[Category: Michels, P A.M]] | + | [[Category: Michels PAM]] |
| - | [[Category: Sakamoto, K]] | + | [[Category: Sakamoto K]] |
| - | [[Category: Shiba, T]] | + | [[Category: Shiba T]] |
| - | [[Category: Tokumasu, F]] | + | [[Category: Tokumasu F]] |
| - | [[Category: Tokuoka, S M]] | + | [[Category: Tokuoka SM]] |
| - | [[Category: African trypanosome]]
| + | |
| - | [[Category: Phosphatase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
D3KVM3_TRYBG
Publication Abstract from PubMed
BACKGROUND: In general, glycerol kinases (GKs) are transferases that catalyze phospho group transfer from ATP to glycerol, and the mechanism was suggested to be random bi-bi. The reverse reaction i.e. phospho transfer from glycerol 3-phosphate (G3P) to ADP is only physiologically feasible by the African trypanosome GK. In contrast to other GKs the mechanism of Trypanosoma brucei gambiense glycerol kinase (TbgGK) was shown to be in an ordered fashion, and proceeding via autophosphorylation. From the unique reaction mechanism of TbgGK, we envisaged its potential to possess phosphatase activity in addition to being a kinase. METHODS: Our hypothesis was tested by spectrophotometric and LC-MS/MS analyses using paranitrophenyl phosphate (pNPP) and TbgGK's natural substrate, G3P respectively. Furthermore, protein X-ray crystallography and site-directed mutagenesis were performed to examine pNPP binding, catalytic residues, and the possible reaction mechanism. RESULTS: In addition to its widely known and expected phosphotransferase (class II) activity, TbgGK can efficiently facilitate the hydrolytic cleavage of phosphoric anhydride bonds (a class III property). This phosphatase activity followed the classical Michaelis-Menten pattern and was competitively inhibited by ADP and G3P, suggesting a common catalytic site for both activities (phosphatase and kinase). The structure of the TGK-pNPP complex, and structure-guided mutagenesis implicated T276 to be important for the catalysis. Remarkably, we captured a crystallographic molecular snapshot of the phosphorylated T276 reaction intermediate. CONCLUSION: We conclude that TbgGK has both kinase and phosphatase activities. GENERAL SIGNIFICANCE: This is the first report on a bifunctional kinase/phosphatase enzyme among members of the sugar kinase family.
Glycerol kinase of African trypanosomes possesses an intrinsic phosphatase activity.,Balogun EO, Inaoka DK, Shiba T, Tokuoka SM, Tokumasu F, Sakamoto K, Kido Y, Michels PAM, Watanabe YI, Harada S, Kita K Biochim Biophys Acta Gen Subj. 2017 Nov;1861(11 Pt A):2830-2842. doi:, 10.1016/j.bbagen.2017.07.028. Epub 2017 Aug 2. PMID:28778484[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Balogun EO, Inaoka DK, Shiba T, Tokuoka SM, Tokumasu F, Sakamoto K, Kido Y, Michels PAM, Watanabe YI, Harada S, Kita K. Glycerol kinase of African trypanosomes possesses an intrinsic phosphatase activity. Biochim Biophys Acta Gen Subj. 2017 Nov;1861(11 Pt A):2830-2842. doi:, 10.1016/j.bbagen.2017.07.028. Epub 2017 Aug 2. PMID:28778484 doi:http://dx.doi.org/10.1016/j.bbagen.2017.07.028
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