1fzi: Difference between revisions

Revision as of 13:44, 21 February 2008

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 with and as ligands. Active as Methane monooxygenase, with EC number 1.14.13.25 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

Page seeded by OCA on Thu Feb 21 12:44:19 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1fzi.gif|left|200px]]<br /><applet load="1fzi" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fzi.gif|left|200px]]<br /><applet load="1fzi" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fzi, resolution 3.30&Aring;" />
 '''METHANE MONOOXYGENASE HYDROXYLASE, FORM I PRESSURIZED WITH XENON GAS'''<br />
 ==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.
+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==
-FZI 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 and XE 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FZI OCA].
+FZI 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> and <scene name='pdbligand=XE:'>XE</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=1FZI OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Methylococcus capsulatus]]
 [[Category: Protein complex]]
-[[Category: Frederick, C.A.]]
+[[Category: Frederick, C A.]]
-[[Category: Lippard, S.J.]]
+[[Category: Lippard, S J.]]
-[[Category: Rosenzweig, A.C.]]
+[[Category: Rosenzweig, A C.]]
-[[Category: Whittington, D.A.]]
+[[Category: Whittington, D A.]]
 [[Category: FE]]
 [[Category: XE]]
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 [[Category: monooxygenase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:32:07 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:44:19 2008''