1fzi
From Proteopedia
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| , resolution 3.30Å | |||||||
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| Ligands: | , | ||||||
| Activity: | Methane monooxygenase, with EC number 1.14.13.25 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
METHANE MONOOXYGENASE HYDROXYLASE, FORM I PRESSURIZED WITH XENON GAS
Overview
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.
About this Structure
1FZI is a Protein complex structure of sequences from Methylococcus capsulatus. Full crystallographic information is available from OCA.
Reference
Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase., Whittington DA, Rosenzweig AC, Frederick CA, Lippard SJ, Biochemistry. 2001 Mar 27;40(12):3476-82. PMID:11297413
Page seeded by OCA on Sun Mar 30 20:33:19 2008
