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| | ==NMR solution structure of a-lytic protease using two 4D-spectra== | | ==NMR solution structure of a-lytic protease using two 4D-spectra== |
| - | <StructureSection load='5wot' size='340' side='right'caption='[[5wot]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='5wot' size='340' side='right'caption='[[5wot]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wot]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WOT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WOT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wot]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WOT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WOT 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/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </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=5wot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wot OCA], [https://pdbe.org/5wot PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wot RCSB], [https://www.ebi.ac.uk/pdbsum/5wot PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wot 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=5wot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wot OCA], [http://pdbe.org/5wot PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wot RCSB], [http://www.ebi.ac.uk/pdbsum/5wot PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wot ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PRLA_LYSEN PRLA_LYSEN] |
| | <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: Alpha-lytic endopeptidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Lysobacter enzymogenes]] | | [[Category: Lysobacter enzymogenes]] |
| - | [[Category: Evangelidis, T]] | + | [[Category: Evangelidis T]] |
| - | [[Category: Nerli, S]] | + | [[Category: Nerli S]] |
| - | [[Category: Sgourakis, N G]] | + | [[Category: Sgourakis NG]] |
| - | [[Category: Tripsianes, K]] | + | [[Category: Tripsianes K]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Protease]]
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| Structural highlights
Function
PRLA_LYSEN
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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