1fzi: Difference between revisions
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[[Image:1fzi.gif|left|200px]] | [[Image:1fzi.gif|left|200px]] | ||
'''METHANE MONOOXYGENASE HYDROXYLASE, FORM I PRESSURIZED WITH XENON GAS''' | {{Structure | ||
|PDB= 1fzi |SIZE=350|CAPTION= <scene name='initialview01'>1fzi</scene>, resolution 3.30Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=XE:XENON'>XE</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Methane_monooxygenase Methane monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.25 1.14.13.25] | |||
|GENE= | |||
}} | |||
'''METHANE MONOOXYGENASE HYDROXYLASE, FORM I PRESSURIZED WITH XENON GAS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1FZI is a [ | 1FZI is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FZI OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11297413 11297413] | ||
[[Category: Methane monooxygenase]] | [[Category: Methane monooxygenase]] | ||
[[Category: Methylococcus capsulatus]] | [[Category: Methylococcus capsulatus]] | ||
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[[Category: monooxygenase]] | [[Category: monooxygenase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:16:05 2008'' | ||
Revision as of 12:16, 20 March 2008
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| , resolution 3.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Methane monooxygenase, with EC number 1.14.13.25 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
METHANE MONOOXYGENASE HYDROXYLASE, FORM I PRESSURIZED WITH XENON GAS
OverviewOverview
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 StructureAbout this Structure
1FZI is a Protein complex structure of sequences from Methylococcus capsulatus. Full crystallographic information is available from OCA.
ReferenceReference
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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