1fzi
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(New page: 200px<br /><applet load="1fzi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fzi, resolution 3.30Å" /> '''METHANE MONOOXYGENAS...)
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Revision as of 13:24, 20 November 2007
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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 with FE and XE as ligands. Active as Methane monooxygenase, with EC number 1.14.13.25 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
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