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| | {{STRUCTURE_2jbr| PDB=2jbr | SCENE= }} | | {{STRUCTURE_2jbr| PDB=2jbr | SCENE= }} |
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| - | '''STRUCTURE OF THE MONOOXYGENASE COMPONENT OF P-HYDROXYPHENYLACETATE HYDROXYLASE FROM ACINETOBACTER BAUMANNI'''
| + | ===STRUCTURE OF THE MONOOXYGENASE COMPONENT OF P-HYDROXYPHENYLACETATE HYDROXYLASE FROM ACINETOBACTER BAUMANNI=== |
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| - | ==Overview==
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| - | p-Hydroxyphenylacetate hydroxylase from Acinetobacter baumannii is a two-component system consisting of a NADH-dependent FMN reductase and a monooxygenase (C2) that uses reduced FMN as substrate. The crystal structures of C2 in the ligand-free and substrate-bound forms reveal a preorganized pocket that binds reduced FMN without large conformational changes. The Phe-266 side chain swings out to provide the space for binding p-hydroxyphenylacetate that is oriented orthogonal to the flavin ring. The geometry of the substrate-binding site of C2 is significantly different from that of p-hydroxybenzoate hydroxylase, a single-component flavoenzyme that catalyzes a similar reaction. The C2 overall structure resembles the folding of medium-chain acyl-CoA dehydrogenase. An outstanding feature in the C2 structure is a cavity located in front of reduced FMN; it has a spherical shape with a 1.9-A radius and a 29-A3 volume and is interposed between the flavin C4a atom and the substrate atom to be hydroxylated. The shape and position of this cavity are perfectly fit for housing the oxygen atoms of the flavin C4a-hydroperoxide intermediate that is formed upon reaction of the C2-bound reduced flavin with molecular oxygen. The side chain of His-396 is predicted to act as a hydrogen-bond donor to the oxygen atoms of the intermediate. This architecture promotes the nucleophilic attack of the substrate onto the terminal oxygen of the hydroperoxyflavin. Comparative analysis with the structures of other flavoenzymes indicates that a distinctive feature of monooxygenases is the presence of specific cavities that encapsulate and stabilize the crucial hydroperoxyflavin intermediate.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17227849}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17227849 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17227849}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Flavoenzyme hydroxylase]] | | [[Category: Flavoenzyme hydroxylase]] |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:39:27 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:25:17 2008'' |
Revision as of 21:25, 27 July 2008
Template:STRUCTURE 2jbr
STRUCTURE OF THE MONOOXYGENASE COMPONENT OF P-HYDROXYPHENYLACETATE HYDROXYLASE FROM ACINETOBACTER BAUMANNI
Template:ABSTRACT PUBMED 17227849
About this Structure
2JBR is a Single protein structure of sequence from Acinetobacter baumannii. Full crystallographic information is available from OCA.
Reference
Structure of the monooxygenase component of a two-component flavoprotein monooxygenase., Alfieri A, Fersini F, Ruangchan N, Prongjit M, Chaiyen P, Mattevi A, Proc Natl Acad Sci U S A. 2007 Jan 23;104(4):1177-82. Epub 2007 Jan 16. PMID:17227849
Page seeded by OCA on Mon Jul 28 00:25:17 2008
