1FZH

METHANE MONOOXYGENASE HYDROXYLASE, FORM II PRESSURIZED WITH XENON GAS

Summary for 1FZH

• Entry DOI: 10.2210/pdb1fzh/pdb
• Descriptor: METHANE MONOOXYGENASE COMPONENT A, ALPHA CHAIN, METHANE MONOOXYGENASE COMPONENT A, BETA CHAIN, METHANE MONOOXYGENASE COMPONENT A, GAMMA CHAIN, ... (7 entities in total)
• Functional Keywords: dinuclear iron center, monooxygenase, oxidoreductase
• Biological source: Methylococcus capsulatus; More
• Total number of polymer chains: 6
• Total formula weight: 253394.93

Authors

Whittington, D.A.,Rosenzweig, A.C.,Frederick, C.A.,Lippard, S.J. (deposition date: 2000-10-03, release date: 2001-04-27, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)