1ckv
From Proteopedia
(New page: 200px<br /><applet load="1ckv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ckv" /> '''STRUCTURE OF THE SOLUBLE METHANE MONOOXYGENA...) |
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| - | [[Image:1ckv.gif|left|200px]]<br /><applet load="1ckv" size=" | + | [[Image:1ckv.gif|left|200px]]<br /><applet load="1ckv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ckv" /> | caption="1ckv" /> | ||
'''STRUCTURE OF THE SOLUBLE METHANE MONOOXYGENASE REGULATORY PROTEIN B'''<br /> | '''STRUCTURE OF THE SOLUBLE METHANE MONOOXYGENASE REGULATORY PROTEIN B'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The soluble methane monooxygenase (sMMO; EC 1.14.13.25) from the | + | The soluble methane monooxygenase (sMMO; EC 1.14.13.25) from the pseudothermophile Methylococcus capsulatus (Bath) is a three-component enzyme system that catalyzes the selective oxidation of methane to methanol. We have used NMR spectroscopy to produce a highly refined structure of MMOB, the 16-kDa regulatory protein of this system. This structure has a unique and intricate fold containing seven beta-strands forming two beta-sheets oriented perpendicular to each other and bridged by three alpha-helices. The rate and efficiency of the methane hydroxylation by sMMO depend on dynamic binding interactions of the hydroxylase with the reductase and regulatory protein components during catalysis. We have monitored by NMR the binding of MMOB to the hydroxylase in the presence and absence of the reductase. The results of these studies provide structural insight into how the regulatory protein interacts with the hydroxylase. |
==About this Structure== | ==About this Structure== | ||
| - | 1CKV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1CKV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gassner, G | + | [[Category: Gassner, G T.]] |
| - | [[Category: Lippard, S | + | [[Category: Lippard, S J.]] |
[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
| - | [[Category: Walters, K | + | [[Category: Walters, K J.]] |
[[Category: hydroxylase regulatory protein]] | [[Category: hydroxylase regulatory protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:06 2008'' |
Revision as of 10:07, 21 February 2008
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STRUCTURE OF THE SOLUBLE METHANE MONOOXYGENASE REGULATORY PROTEIN B
Overview
The soluble methane monooxygenase (sMMO; EC 1.14.13.25) from the pseudothermophile Methylococcus capsulatus (Bath) is a three-component enzyme system that catalyzes the selective oxidation of methane to methanol. We have used NMR spectroscopy to produce a highly refined structure of MMOB, the 16-kDa regulatory protein of this system. This structure has a unique and intricate fold containing seven beta-strands forming two beta-sheets oriented perpendicular to each other and bridged by three alpha-helices. The rate and efficiency of the methane hydroxylation by sMMO depend on dynamic binding interactions of the hydroxylase with the reductase and regulatory protein components during catalysis. We have monitored by NMR the binding of MMOB to the hydroxylase in the presence and absence of the reductase. The results of these studies provide structural insight into how the regulatory protein interacts with the hydroxylase.
About this Structure
1CKV is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of the soluble methane monooxygenase regulatory protein B., Walters KJ, Gassner GT, Lippard SJ, Wagner G, Proc Natl Acad Sci U S A. 1999 Jul 6;96(14):7877-82. PMID:10393915
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