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| | ==NMR solution structure of Enzyme I (nEIt) protein using two 4D-spectra== | | ==NMR solution structure of Enzyme I (nEIt) protein using two 4D-spectra== |
| - | <StructureSection load='5woy' size='340' side='right'caption='[[5woy]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='5woy' size='340' side='right'caption='[[5woy]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5woy]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WOY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5WOY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5woy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis_MB4 Caldanaerobacter subterraneus subsp. tengcongensis MB4]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WOY FirstGlance]. <br> |
| - | </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> | + | </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=5woy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5woy OCA], [https://pdbe.org/5woy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5woy RCSB], [https://www.ebi.ac.uk/pdbsum/5woy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5woy 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=5woy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5woy OCA], [http://pdbe.org/5woy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5woy RCSB], [http://www.ebi.ac.uk/pdbsum/5woy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5woy 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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Caldanaerobacter subterraneus subsp. tengcongensis MB4]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphoenolpyruvate--protein phosphotransferase]]
| + | [[Category: Evangelidis T]] |
| - | [[Category: Evangelidis, T]] | + | [[Category: Nerli S]] |
| - | [[Category: Nerli, S]] | + | [[Category: Sgourakis NG]] |
| - | [[Category: Sgourakis, N G]] | + | [[Category: Tripsianes K]] |
| - | [[Category: Tripsianes, K]] | + | |
| - | [[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
Automated methods for NMR structure determination of proteins are continuously becoming more robust. However, current methods addressing larger, more complex targets rely on analyzing 6-10 complementary spectra, suggesting the need for alternative approaches. Here, we describe 4D-CHAINS/autoNOE-Rosetta, a complete pipeline for NOE-driven structure determination of medium- to larger-sized proteins. The 4D-CHAINS algorithm analyzes two 4D spectra recorded using a single, fully protonated protein sample in an iterative ansatz where common NOEs between different spin systems supplement conventional through-bond connectivities to establish assignments of sidechain and backbone resonances at high levels of completeness and with a minimum error rate. The 4D-CHAINS assignments are then used to guide automated assignment of long-range NOEs and structure refinement in autoNOE-Rosetta. Our results on four targets ranging in size from 15.5 to 27.3 kDa illustrate that the structures of proteins can be determined accurately and in an unsupervised manner in a matter of days.
Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra.,Evangelidis T, Nerli S, Novacek J, Brereton AE, Karplus PA, Dotas RR, Venditti V, Sgourakis NG, Tripsianes K Nat Commun. 2018 Jan 26;9(1):384. doi: 10.1038/s41467-017-02592-z. PMID:29374165[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Evangelidis T, Nerli S, Novacek J, Brereton AE, Karplus PA, Dotas RR, Venditti V, Sgourakis NG, Tripsianes K. Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra. Nat Commun. 2018 Jan 26;9(1):384. doi: 10.1038/s41467-017-02592-z. PMID:29374165 doi:http://dx.doi.org/10.1038/s41467-017-02592-z
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