2mx8

NMR structure of N-terminal domain from A. ventricosus minor ampullate spidroin (MiSp) at pH 7.2

spinqualitylabelsall models 2mx8 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mx8 is a 1 chain structure with sequence from Araneus ventricosus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function K4MTL7_ARAVE Publication Abstract from PubMed Conversion of spider silk proteins from soluble dope to insoluble fibers involves pH-dependent dimerization of the N-terminal domain (NT). This conversion is tightly regulated to prevent premature precipitation and enable rapid silk formation at the end of the duct. Three glutamic acid residues that mediate this process in the NT from Euprosthenops australis major ampullate spidroin 1 are well conserved among spidroins. However, NTs of minor ampullate spidroins from several species, including Araneus ventricosus ((Av) MiSp NT), lack one of the glutamic acids. Here we investigate the pH-dependent structural changes of (Av) MiSp NT, revealing that it uses the same mechanism but involves a non-conserved glutamic acid residue instead. Homology modeling of the structures of other MiSp NTs suggests that these harbor different compensatory residues. This indicates that, despite sequence variations, the molecular mechanism underlying pH-dependent dimerization of NT is conserved among different silk types. Diversified Structural Basis of a Conserved Molecular Mechanism for pH-Dependent Dimerization in Spider Silk N-Terminal Domains.,Otikovs M, Chen G, Nordling K, Landreh M, Meng Q, Jornvall H, Kronqvist N, Rising A, Johansson J, Jaudzems K Chembiochem. 2015 Aug 17;16(12):1720-4. doi: 10.1002/cbic.201500263. Epub 2015, Jul 1. PMID:26033527 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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