1JTN
Alternative Structures of a Sequence Extended T4 Lysozyme Show that the Highly Conserved Beta-Sheet Region has weak intrinsic Folding Propensity
Summary for 1JTN
| Entry DOI | 10.2210/pdb1jtn/pdb |
| Related | 1JTM |
| Descriptor | LYSOZYME, SULFATE ION (3 entities in total) |
| Functional Keywords | sequence duplication, context dependent folding, sequence repeat, hydrolase |
| Biological source | Enterobacteria phage T4 |
| Total number of polymer chains | 2 |
| Total formula weight | 40634.53 |
| Authors | Sagermann, M.,Matthews, B.W. (deposition date: 2001-08-21, release date: 2002-03-20, Last modification date: 2023-08-16) |
| Primary citation | Sagermann, M.,Matthews, B.W. Crystal Structures of a T4-lysozyme Duplication-extension Mutant Demonstrate that the Highly Conserved beta-Sheet Region has Low Intrinsic Folding Propensity J.Mol.Biol., 316:931-940, 2002 Cited by PubMed Abstract: 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. PubMed: 11884133DOI: 10.1006/jmbi.2001.5376 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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