PDBsum entry 1fz8

Oxidoreductase

PDB id: 1fz8

Contents

Protein chains

511 a.a. *

388 a.a. *

167 a.a. *

Ligands

2BM ×10

Metals

_FE ×4

_CA ×3

Waters ×1069

* Residue conservation analysis

References listed in PDB file

Key reference

• Title: Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase.
• Authors: D.A.Whittington, A.C.Rosenzweig, C.A.Frederick, S.J.Lippard.
• Ref.: Biochemistry, 2001, 40, 3476-3482. [DOI no: 10.1021/bi0022487]
• PubMed id: 11297413

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.