1sts
From Proteopedia
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| - | [[Image:1sts.gif|left|200px]] | + | [[Image:1sts.gif|left|200px]] |
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| - | '''STREPTAVIDIN DIMERIZED BY DISULFIDE-BONDED PEPTIDE FCHPQNT-NH2 DIMER''' | + | {{Structure |
| + | |PDB= 1sts |SIZE=350|CAPTION= <scene name='initialview01'>1sts</scene>, resolution 1.95Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STREPTAVIDIN DIMERIZED BY DISULFIDE-BONDED PEPTIDE FCHPQNT-NH2 DIMER''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1STS is a [ | + | 1STS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1STS OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8537386 8537386] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces avidinii]] | [[Category: Streptomyces avidinii]] | ||
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[[Category: complex (glycoprotein/peptide)]] | [[Category: complex (glycoprotein/peptide)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:09:32 2008'' |
Revision as of 12:09, 20 March 2008
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| , resolution 1.95Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STREPTAVIDIN DIMERIZED BY DISULFIDE-BONDED PEPTIDE FCHPQNT-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
1STS is a Single protein structure of sequence from Streptomyces avidinii. 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 Thu Mar 20 14:09:32 2008
