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| | <StructureSection load='6vbj' size='340' side='right'caption='[[6vbj]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='6vbj' size='340' side='right'caption='[[6vbj]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6vbj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/As_1.2430 As 1.2430]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VBJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VBJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6vbj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis Caldanaerobacter subterraneus subsp. tengcongensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VBJ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PtsA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=119072 AS 1.2430])</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]] 2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate--protein_phosphotransferase Phosphoenolpyruvate--protein phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.9 2.7.3.9] </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=6vbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vbj OCA], [https://pdbe.org/6vbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vbj RCSB], [https://www.ebi.ac.uk/pdbsum/6vbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vbj ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vbj OCA], [http://pdbe.org/6vbj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vbj RCSB], [http://www.ebi.ac.uk/pdbsum/6vbj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vbj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q8R7R4_CALS4 Q8R7R4_CALS4]] General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).[PIRNR:PIRNR000732] | + | [https://www.uniprot.org/uniprot/Q8R7R4_CALS4 Q8R7R4_CALS4] General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).[PIRNR:PIRNR000732] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6vbj" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6vbj" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Phosphotransferase 3D structures|Phosphotransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: As 1 2430]] | + | [[Category: Caldanaerobacter subterraneus subsp. tengcongensis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphoenolpyruvate--protein phosphotransferase]]
| + | [[Category: Stewart Jr CE]] |
| - | [[Category: Stewart, C E]] | + | |
| - | [[Category: Bacterial phosphotransferase]]
| + | |
| - | [[Category: Hybrid]]
| + | |
| - | [[Category: Phosphoenolpyruvate-protein phosphotransferase ptsi]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q8R7R4_CALS4 General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).[PIRNR:PIRNR000732]
Publication Abstract from PubMed
Conformational disorder is emerging as an important feature of biopolymers, regulating a vast array of cellular functions, including signaling, phase separation, and enzyme catalysis. Here we combine NMR, crystallography, computer simulations, protein engineering, and functional assays to investigate the role played by conformational heterogeneity in determining the activity of the C-terminal domain of bacterial Enzyme I (EIC). In particular, we design chimeric proteins by hybridizing EIC from thermophilic and mesophilic organisms, and we characterize the resulting constructs for structure, dynamics, and biological function. We show that EIC exists as a mixture of active and inactive conformations and that functional regulation is achieved by tuning the thermodynamic balance between active and inactive states. Interestingly, we also present a hybrid thermophilic/mesophilic enzyme that is thermostable and more active than the wild-type thermophilic enzyme, suggesting that hybridizing thermophilic and mesophilic proteins is a valid strategy to engineer thermostable enzymes with significant low-temperature activity.
Hybrid thermophilic/mesophilic enzymes reveal a role for conformational disorder in regulation of bacterial Enzyme I.,Dotas RR, Nguyen TT, Stewart CE Jr, Ghirlando R, Potoyan DA, Venditti V J Mol Biol. 2020 Jun 3. pii: S0022-2836(20)30375-2. doi:, 10.1016/j.jmb.2020.05.024. PMID:32504625[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dotas RR, Nguyen TT, Stewart CE Jr, Ghirlando R, Potoyan DA, Venditti V. Hybrid thermophilic/mesophilic enzymes reveal a role for conformational disorder in regulation of bacterial Enzyme I. J Mol Biol. 2020 Jun 3. pii: S0022-2836(20)30375-2. doi:, 10.1016/j.jmb.2020.05.024. PMID:32504625 doi:http://dx.doi.org/10.1016/j.jmb.2020.05.024
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