High-resolution structure of an alpha-spectrin SH3-domain mutant with a redesigned hydrophobic core.
The alpha-spectrin SH3 domain (Spc-SH3) is a small modular domain which has been broadly used as a model protein in folding studies and these studies have sometimes been supported by structural information obtained from the coordinates of Spc-SH3 mutants. The structure of B5/D48G, a multiple mutant designed to improve the hydrophobic core and as a consequence the protein stability, has been solved at 1 A resolution. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a=24.79, b=37.23, c=62.95 A. This mutant also bears a D48G substitution in the distal loop and this mutation has also been reported to increase the stability of the protein by itself. The structure of the B5/D48G mutant shows a highly packed hydrophobic core and a more ordered distal loop compared with previous Spc-SH3 structures.
Cámara-Artigas
Ana
A
Departamento de Química-Física, Bioquímica y Química Inorgánica, Universidad de Almería, Carretera Sacramento, Almería 04120, Spain. acamara@ual.es
Andújar-Sánchez
Monserrat
M
Ortiz-Salmerón
Emilia
E
Cuadri
Celia
C
Cobos
Eva S
ES
Martin-Garcia
Jose Manuel
JM
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D009154:Mutation; D016415:Sequence Alignment; D013049:Spectrin / Q000737:chemistry* / Q000235:genetics; D018909:src Homology Domains
D013049:Spectrin
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