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| ==NMR structure of major ampullate spidroin 1 N-terminal domain at pH 5.5== | | ==NMR structure of major ampullate spidroin 1 N-terminal domain at pH 5.5== |
- | <StructureSection load='2lth' size='340' side='right' caption='[[2lth]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lth' size='340' side='right'caption='[[2lth]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2lth]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Euprosthenops_australis Euprosthenops australis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LTH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LTH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lth]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Euprosthenops_australis Euprosthenops australis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LTH FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MaSp1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=332052 Euprosthenops australis])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lth OCA], [http://pdbe.org/2lth PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lth RCSB], [http://www.ebi.ac.uk/pdbsum/2lth PDBsum]</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=2lth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lth OCA], [https://pdbe.org/2lth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lth RCSB], [https://www.ebi.ac.uk/pdbsum/2lth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lth ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q05H60_9ARAC Q05H60_9ARAC] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </StructureSection> | | </StructureSection> |
| [[Category: Euprosthenops australis]] | | [[Category: Euprosthenops australis]] |
- | [[Category: Askarieh, G]] | + | [[Category: Large Structures]] |
- | [[Category: Jaudzems, K]] | + | [[Category: Askarieh G]] |
- | [[Category: Johansson, J]] | + | [[Category: Jaudzems K]] |
- | [[Category: Knight, S]] | + | [[Category: Johansson J]] |
- | [[Category: Landreh, M]] | + | [[Category: Knight S]] |
- | [[Category: Nordling, K]] | + | [[Category: Landreh M]] |
- | [[Category: Otikovs, M]] | + | [[Category: Nordling K]] |
- | [[Category: Rising, A]] | + | [[Category: Otikovs M]] |
- | [[Category: Structural protein]]
| + | [[Category: Rising A]] |
| Structural highlights
Function
Q05H60_9ARAC
Publication Abstract from PubMed
The mechanisms controlling the conversion of spider silk proteins into insoluble fibres, which happens in a fraction of a second and in a defined region of the silk glands, are still unresolved. The N-terminal domain changes conformation and forms a homodimer when pH is lowered from 7 to 6; however, the molecular details still remain to be determined. Here we investigate site-directed mutants of the N-terminal domain from Euprosthenops australis major ampullate spidroin 1 and find that the charged residues D40, R60 and K65 mediate intersubunit electrostatic interactions. Protonation of E79 and E119 is required for structural conversions of the subunits into a dimer conformation, and subsequent protonation of E84 around pH 5.7 leads to the formation of a fully stable dimer. These residues are highly conserved, indicating that the now proposed three-step mechanism prevents premature aggregation of spidroins and enables fast formation of spider silk fibres in general.
Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation.,Kronqvist N, Otikovs M, Chmyrov V, Chen G, Andersson M, Nordling K, Landreh M, Sarr M, Jornvall H, Wennmalm S, Widengren J, Meng Q, Rising A, Otzen D, Knight SD, Jaudzems K, Johansson J Nat Commun. 2014 Feb 10;5:3254. doi: 10.1038/ncomms4254. PMID:24510122[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kronqvist N, Otikovs M, Chmyrov V, Chen G, Andersson M, Nordling K, Landreh M, Sarr M, Jornvall H, Wennmalm S, Widengren J, Meng Q, Rising A, Otzen D, Knight SD, Jaudzems K, Johansson J. Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation. Nat Commun. 2014 Feb 10;5:3254. doi: 10.1038/ncomms4254. PMID:24510122 doi:http://dx.doi.org/10.1038/ncomms4254
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