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ABSTRACT:
SUBMITTER: Le Trong I
PROVIDER: S-EPMC3663120 | biostudies-literature | 2013 Jun
REPOSITORIES: biostudies-literature
Le Trong Isolde I Chu Vano V Xing Yi Y Lybrand Terry P TP Stayton Patrick S PS Stenkamp Ronald E RE
Acta crystallographica. Section D, Biological crystallography 20130511 Pt 6
Circular permutation of streptavidin was carried out in order to investigate the role of a main-chain amide in stabilizing the high-affinity complex of the protein and biotin. Mutant proteins CP49/48 and CP50/49 were constructed to place new N-termini at residues 49 and 50 in a flexible loop involved in stabilizing the biotin complex. Crystal structures of the two mutants show that half of each loop closes over the binding site, as observed in wild-type streptavidin, while the other half adopts ...[more]