1jtn
From Proteopedia
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Alternative Structures of a Sequence Extended T4 Lysozyme Show that the Highly Conserved Beta-Sheet Region has weak intrinsic Folding Propensity
Overview
Residues 24 to 35 of T4 lysozyme correspond to the second and third, strands of a region of beta-sheet that is highly conserved in all known, lysozyme and chitinase structures. To evaluate the intrinsic propensity of, these amino acid residues to form a defined structure they were added at, the C terminus of the native protein, together with a dipeptide linker., Two crystal structures of this active, mutant protein were obtained, to, 1.9A and 2.3A resolution, respectively. Even though the crystal conditions, are similar, the appended sequence adopts very different secondary, structures. In one case it is weakly structured and appears to extend, through the active-site cleft, perhaps in part adding an extra strand to, the original beta-sheet. In the other crystal form the extension is, largely alpha-helical. The formation of these alternative structures shows, that the sequence does not have a strong intrinsic propensity to form a, unique fold (either beta-sheet or otherwise). The results also suggest, that structural conservation during evolution does not necessarily depend, on sequence conservation or the conservation of folding propensity.
About this Structure
1JTN is a Single protein structure of sequence from Bacteriophage t4 with SO4 as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Crystal structures of a T4-lysozyme duplication-extension mutant demonstrate that the highly conserved beta-sheet region has low intrinsic folding propensity., Sagermann M, Matthews BW, J Mol Biol. 2002 Mar 1;316(4):931-40. PMID:11884133
Page seeded by OCA on Tue Nov 20 18:34:14 2007
