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1STR

STREPTAVIDIN DIMERIZED BY DISULFIDE-BONDED PEPTIDE AC-CHPQNT-NH2 DIMER

1STR の概要
エントリーDOI10.2210/pdb1str/pdb
分子名称STREPTAVIDIN, AC-CHPQNT-NH2 (3 entities in total)
機能のキーワードcomplex (glycoprotein-peptide), complex (glycoprotein-peptide) complex, complex (glycoprotein/peptide)
由来する生物種Streptomyces avidinii
細胞内の位置Secreted: P22629
タンパク質・核酸の鎖数4
化学式量合計27377.65
構造登録者
Katz, B.A.,Cass, R.T.,Liu, B.,Arze, R.,Collins, N. (登録日: 1995-09-12, 公開日: 1996-03-08, 最終更新日: 2024-11-13)
主引用文献Katz, B.A.,Cass, R.T.,Liu, B.,Arze, R.,Collins, N.
Topochemical catalysis achieved by structure-based ligand design.
J.Biol.Chem., 270:31210-31218, 1995
Cited by
PubMed Abstract: 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.
PubMed: 8537386
DOI: 10.1074/jbc.270.52.31210
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.8 Å)
構造検証レポート
Validation report summary of 1str
検証レポート(詳細版)ダウンロードをダウンロード

250059

件を2026-03-04に公開中

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