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| - | [[Image:2vq7.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2vq7| PDB=2vq7 | SCENE= }} | | {{STRUCTURE_2vq7| PDB=2vq7 | SCENE= }} |
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| - | '''BACTERIAL FLAVIN-CONTAINING MONOOXYGENASE IN COMPLEX WITH NADP: NATIVE DATA'''
| + | ===BACTERIAL FLAVIN-CONTAINING MONOOXYGENASE IN COMPLEX WITH NADP: NATIVE DATA=== |
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| - | ==Overview==
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| - | Flavin-containing monooxygenases (FMOs) are, after cytochromes P450, the most important monooxygenase system in humans and are involved in xenobiotics metabolism and variability in drug response. The x-ray structure of a soluble prokaryotic FMO from Methylophaga sp. strain SK1 has been solved at 2.6-A resolution and is now the protein of known structure with the highest sequence similarity to human FMOs. The structure possesses a two-domain architecture, with both FAD and NADP(+) well defined by the electron density maps. Biochemical analysis shows that the prokaryotic enzyme shares many functional properties with mammalian FMOs, including substrate specificity and the ability to stabilize the hydroperoxyflavin intermediate that is crucial in substrate oxygenation. On the basis of their location in the structure, the nicotinamide ring and the adjacent ribose of NADP(+) turn out to be an integral part of the catalytic site being actively engaged in the stabilization of the oxygenating intermediate. This feature suggests that NADP(H) has a moonlighting role, in that it adopts two binding modes that allow it to function in both flavin reduction and oxygen reactivity modulation, respectively. We hypothesize that a relative domain rotation is needed to bring NADP(H) to these distinct positions inside the active site. Localization of mutations in human FMO3 that are known to cause trimethylaminuria (fish-odor syndrome) in the elucidated FMO structure provides a structural explanation for their biological effects.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_18443301}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 18443301 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_18443301}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| | [[Category: Oxygen]] | | [[Category: Oxygen]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 14 11:40:16 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:01:15 2008'' |
Revision as of 07:01, 29 July 2008
Template:STRUCTURE 2vq7
BACTERIAL FLAVIN-CONTAINING MONOOXYGENASE IN COMPLEX WITH NADP: NATIVE DATA
Template:ABSTRACT PUBMED 18443301
About this Structure
2VQ7 is a Single protein structure of sequence from Methylophaga sp. sk1. Full crystallographic information is available from OCA.
Reference
Revealing the moonlighting role of NADP in the structure of a flavin-containing monooxygenase., Alfieri A, Malito E, Orru R, Fraaije MW, Mattevi A, Proc Natl Acad Sci U S A. 2008 May 6;105(18):6572-7. Epub 2008 Apr 28. PMID:18443301
Page seeded by OCA on Tue Jul 29 10:01:15 2008
