1FZ8

METHANE MONOOXYGENASE HYDROXYLASE, FORM II COCRYSTALLIZED WITH DIBROMOMETHANE

1FZ8 の概要

• エントリーDOI: 10.2210/pdb1fz8/pdb
• 分子名称: METHANE MONOOXYGENASE COMPONENT A, ALPHA CHAIN, METHANE MONOOXYGENASE COMPONENT A, BETA CHAIN, METHANE MONOOXYGENASE COMPONENT A, GAMMA CHAIN, ... (7 entities in total)
• 機能のキーワード: dinuclear iron center, monooxygenase, oxidoreductase
• 由来する生物種: Methylococcus capsulatus; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 253648.97

構造登録者

Whittington, D.A.,Rosenzweig, A.C.,Frederick, C.A.,Lippard, S.J. (登録日: 2000-10-03, 公開日: 2001-04-27, 最終更新日: 2024-02-07)

主引用文献

Whittington, D.A.,Rosenzweig, A.C.,Frederick, C.A.,Lippard, S.J.
Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase.
Biochemistry, 40:3476-3482, 2001

PubMed Abstract: To investigate the role of protein cavities in facilitating movement of the substrates, methane and dioxygen, in the soluble methane monooxygenase hydroxylase (MMOH), we determined the X-ray structures of MMOH from Methylococcus capsulatus (Bath) cocrystallized with dibromomethane or iodoethane, or by using crystals pressurized with xenon gas. The halogenated alkanes bind in two cavities within the alpha-subunit that extend from one surface of the protein to the buried dinuclear iron active site. Two additional binding sites were located in the beta-subunit. Pressurization of two crystal forms of MMOH with xenon resulted in the identification of six binding sites located exclusively in the alpha-subunit. These results indicate that hydrophobic species bind preferentially in preexisting cavities in MMOH and support the hypothesis that such cavities may play a functional role in sequestering and enhancing the availability of the physiological substrates for reaction at the active site.

PubMed: 11297413
DOI: 10.1021/bi0022487

実験手法

X-RAY DIFFRACTION (2.1 Å)