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3HNH

Crystal Structure of PqqC Active Site Mutant Y175S,R179S in complex with a reaction intermediate

3HNH の概要
エントリーDOI10.2210/pdb3hnh/pdb
関連するPDBエントリー1OTV 1OTW 3HLX 3HML
分子名称Pyrroloquinoline-quinone synthase, (2S,7R,9R)-4,5-dihydroxy-2,3,6,7,8,9-hexahydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylic acid (3 entities in total)
機能のキーワードpqqc, pqq biosynthesis, oxidase, complex, all helical, oxidoreductase
由来する生物種Klebsiella pneumoniae subsp. pneumoniae
タンパク質・核酸の鎖数1
化学式量合計30194.98
構造登録者
Puehringer, S.,Schwarzenbacher, R. (登録日: 2009-05-31, 公開日: 2010-05-12, 最終更新日: 2023-11-01)
主引用文献Puehringer, S.,RoseFigura, J.,Metlitzky, M.,Toyama, H.,Klinman, J.P.,Schwarzenbacher, R.
Structural studies of mutant forms of the PQQ-forming enzyme PqqC in the presence of product and substrate
Proteins, 78:2554-2562, 2010
Cited by
PubMed Abstract: Pyrroloquinoline quinone [4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylic acid (PQQ)] is a bacterial cofactor in numerous alcohol dehydrogenases including methanol dehydrogenase and glucose dehydrogenase. Its biosynthesis in Klebsiella pneumoniae is facilitated by six genes, pqqABCDEF and proceeds by an unknown pathway. PqqC is one of two metal free oxidases of known structure and catalyzes the last step of PQQ biogenesis which involves a ring closure and an eight-electron oxidation of the substrate [3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid (AHQQ)]. PqqC has 14 conserved active site residues, which have previously been shown to be in close contact with bound PQQ. Herein, we describe the structures of three PqqC active site variants, H154S, Y175F, and the double mutant R179S/Y175S. The H154S crystal structure shows that, even with PQQ bound, the enzyme is still in the "open" conformation with helices alpha5b and alpha6 unfolded and the active site solvent accessible. The Y175F PQQ complex crystal structure reveals the closed conformation indicating that Y175 is not required for the conformational change. The R179S/Y175S AHQQ complex crystal structure is the most mechanistically informative, indicating an open conformation with a reaction intermediate trapped in the active site. The intermediate seen in R179S/Y175S is tricyclic but nonplanar, implying that it has not undergone oxidation. These studies implicate a stepwise process in which substrate binding leads to the generation of the closed protein conformation, with the latter playing a critical role in O(2) binding and catalysis.
PubMed: 20602352
DOI: 10.1002/prot.22769
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 3hnh
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-06に公開中

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