1str
From Proteopedia
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STREPTAVIDIN DIMERIZED BY DISULFIDE-BONDED PEPTIDE AC-CHPQNT-NH2 DIMER
Overview
Recently, a cyclic peptide ligand, cyclo-Ac-[CHPQG-PPC]-NH2, that binds to, streptavidin with high affinity was discovered by screening phage, libraries. From the streptavidin-bound crystal structures of, cyclo-Ac-[CHPQGPPC]-NH2 and of a related but more weakly binding linear, ligand, FSHPQNT, we designed linear thiol-containing streptavidin binding, ligands, FCH-PQNT-NH2 and Ac-CHPQNT-NH2, which are dimerized catalytically, by the streptavidin crystal lattice of space group I222, as demonstrated, by high performance liquid chromatography and mass spectrometry. The, catalytic dimerization relies on presentation of the ligand thiols toward, one another in the lattice. The streptavidin crystal lattice-mediated, catalysis achieved by structure-based design is the first example of, catalysis of a chemical reaction by a protein crystal lattice. The, spontaneous and crystal catalyzed rates of disulfide formation were, determined by high performance liquid chromatography at pH 3.1, 4.0, 5.0, and 6.0. The ratio of the catalyzed to uncatalyzed rate was maximal at pH, 3.1 (kcat/kuncat = 3.8), diminishing to 1.2 at pH 6.0. The crystal, structures of the streptavidin-bound dimerized peptide ligands, FCHPQNT-NH2 dimer at 1.95 A and Ac-CHPQNT-NH2 dimer at 1.80 A, are, described and compared with the structures of streptavidin-bound FSHPQNT, monomer and cyclo-Ac-[CHPQGPPC]-NH2 dimer.
About this Structure
1STR is a Single protein structure of sequence from Streptomyces avidinii with ACE and NH2 as ligands. Full crystallographic information is available from OCA.
Reference
Topochemical catalysis achieved by structure-based ligand design., Katz BA, Cass RT, Liu B, Arze R, Collins N, J Biol Chem. 1995 Dec 29;270(52):31210-8. PMID:8537386
Page seeded by OCA on Wed Nov 21 02:39:38 2007
