1fz8
From Proteopedia
(New page: 200px<br /><applet load="1fz8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fz8, resolution 2.10Å" /> '''METHANE MONOOXYGENAS...) |
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| - | [[Image:1fz8.gif|left|200px]]<br /><applet load="1fz8" size=" | + | [[Image:1fz8.gif|left|200px]]<br /><applet load="1fz8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fz8, resolution 2.10Å" /> | caption="1fz8, resolution 2.10Å" /> | ||
'''METHANE MONOOXYGENASE HYDROXYLASE, FORM II COCRYSTALLIZED WITH DIBROMOMETHANE'''<br /> | '''METHANE MONOOXYGENASE HYDROXYLASE, FORM II COCRYSTALLIZED WITH DIBROMOMETHANE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | To investigate the role of protein cavities in facilitating movement of | + | 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== | ==About this Structure== | ||
| - | 1FZ8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus] with FE, CA and 2BM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1FZ8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=2BM:'>2BM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FZ8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Methylococcus capsulatus]] | [[Category: Methylococcus capsulatus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Frederick, C | + | [[Category: Frederick, C A.]] |
| - | [[Category: Lippard, S | + | [[Category: Lippard, S J.]] |
| - | [[Category: Rosenzweig, A | + | [[Category: Rosenzweig, A C.]] |
| - | [[Category: Whittington, D | + | [[Category: Whittington, D A.]] |
[[Category: 2BM]] | [[Category: 2BM]] | ||
[[Category: CA]] | [[Category: CA]] | ||
| Line 24: | Line 24: | ||
[[Category: monooxygenase]] | [[Category: monooxygenase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:44:15 2008'' |
Revision as of 10:44, 21 February 2008
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METHANE MONOOXYGENASE HYDROXYLASE, FORM II COCRYSTALLIZED WITH DIBROMOMETHANE
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
1FZ8 is a Protein complex structure of sequences from Methylococcus capsulatus with , and 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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