1str: Difference between revisions
New page: left|200px<br /><applet load="1str" size="450" color="white" frame="true" align="right" spinBox="true" caption="1str, resolution 1.80Å" /> '''STREPTAVIDIN DIMERIZ... |
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[[Image:1str.gif|left|200px]]<br /><applet load="1str" size=" | [[Image:1str.gif|left|200px]]<br /><applet load="1str" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1str, resolution 1.80Å" /> | caption="1str, resolution 1.80Å" /> | ||
'''STREPTAVIDIN DIMERIZED BY DISULFIDE-BONDED PEPTIDE AC-CHPQNT-NH2 DIMER'''<br /> | '''STREPTAVIDIN DIMERIZED BY DISULFIDE-BONDED PEPTIDE AC-CHPQNT-NH2 DIMER'''<br /> | ||
==Overview== | ==Overview== | ||
Recently, a cyclic peptide ligand, cyclo-Ac-[CHPQG-PPC]-NH2, that binds to | 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== | ==About this Structure== | ||
1STR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii] with ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1STR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1STR OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Streptomyces avidinii]] | [[Category: Streptomyces avidinii]] | ||
[[Category: Arze, R.]] | [[Category: Arze, R.]] | ||
[[Category: Cass, R | [[Category: Cass, R T.]] | ||
[[Category: Collins, N.]] | [[Category: Collins, N.]] | ||
[[Category: Katz, B | [[Category: Katz, B A.]] | ||
[[Category: Liu, B.]] | [[Category: Liu, B.]] | ||
[[Category: ACE]] | [[Category: ACE]] | ||
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[[Category: complex (glycoprotein/peptide)]] | [[Category: complex (glycoprotein/peptide)]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:05 2008'' | ||
Revision as of 16:05, 21 February 2008
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STREPTAVIDIN DIMERIZED BY DISULFIDE-BONDED PEPTIDE AC-CHPQNT-NH2 DIMER
OverviewOverview
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 StructureAbout this Structure
1STR is a Single protein structure of sequence from Streptomyces avidinii with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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
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