2jbs

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[[Image:2jbs.gif|left|200px]]<br /><applet load="2jbs" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2jbs.gif|left|200px]]
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caption="2jbs, resolution 2.80&Aring;" />
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'''STRUCTURE OF THE MONOOXYGENASE COMPONENT OF P-HYDROXYPHENYLACETATE HYDROXYLASE FROM ACINETOBACTER BAUMANNII'''<br />
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{{Structure
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|PDB= 2jbs |SIZE=350|CAPTION= <scene name='initialview01'>2jbs</scene>, resolution 2.80&Aring;
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|SITE= <scene name='pdbsite=AC1:Fmn+Binding+Site+For+Chain+D'>AC1</scene>
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|LIGAND= <scene name='pdbligand=FMN:FLAVIN MONONUCLEOTIDE'>FMN</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''STRUCTURE OF THE MONOOXYGENASE COMPONENT OF P-HYDROXYPHENYLACETATE HYDROXYLASE FROM ACINETOBACTER BAUMANNII'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2JBS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii] with <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Fmn+Binding+Site+For+Chain+D'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JBS OCA].
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2JBS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JBS OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17227849 17227849]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17227849 17227849]
[[Category: Acinetobacter baumannii]]
[[Category: Acinetobacter baumannii]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:01:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:39:47 2008''

Revision as of 15:39, 20 March 2008


PDB ID 2jbs

Drag the structure with the mouse to rotate
, resolution 2.80Å
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF THE MONOOXYGENASE COMPONENT OF P-HYDROXYPHENYLACETATE HYDROXYLASE FROM ACINETOBACTER BAUMANNII


Overview

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.

About this Structure

2JBS 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

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