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1F89

Crystal structure of Saccharomyces cerevisiae Nit3, a member of branch 10 of the nitrilase superfamily

1F89 の概要
エントリーDOI10.2210/pdb1f89/pdb
分子名称32.5 KDA PROTEIN YLR351C (2 entities in total)
機能のキーワードnitrilase, dimer, structural genomics, four layer sandwich, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, unknown function
由来する生物種Saccharomyces cerevisiae (baker's yeast)
タンパク質・核酸の鎖数2
化学式量合計65182.43
構造登録者
主引用文献Kumaran, D.,Eswaramoorthy, S.,Gerchman, S.E.,Kycia, H.,Studier, F.W.,Swaminathan, S.
Crystal structure of a putative CN hydrolase from yeast
Proteins, 52:283-291, 2003
Cited by
PubMed Abstract: The crystal structure of a yeast hypothetical protein with sequence similarity to CN hydrolases has been determined to 2.4 A resolution by the multiwavelength anomalous dispersion (MAD) method. The protein folds as a four-layer alphabetabetaalpha sandwich and exists as a dimer in the crystal and in solution. It was selected in a structural genomics project as representative of CN hydrolases at a time when no structures had been determined for members of this family. Structures for two other members of the family have since been reported and the three proteins have similar topology and dimerization modes, which are distinct from those of other alphabetabetaalpha proteins whose structures are known. The dimers form an unusual eight-layer alphabetabetaalpha:alphabetabetaalpha structure. Although the precise enzymatic reactions catalyzed by the yeast protein are not known, considerable information about the active site may be deduced from conserved sequence motifs, comparative biochemical information, and comparison with known structures of hydrolase active sites. As with serine hydrolases, the active-site nucleophile (cysteine in this case) is positioned on a nucleophile elbow.
PubMed: 12833551
DOI: 10.1002/prot.10417
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.4 Å)
構造検証レポート
Validation report summary of 1f89
検証レポート(詳細版)ダウンロードをダウンロード

247035

件を2026-01-07に公開中

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