1bkj

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[[Image:1bkj.gif|left|200px]]<br /><applet load="1bkj" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1bkj.gif|left|200px]]
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caption="1bkj, resolution 1.8&Aring;" />
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'''NADPH:FMN OXIDOREDUCTASE FROM VIBRIO HARVEYI'''<br />
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{{Structure
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|PDB= 1bkj |SIZE=350|CAPTION= <scene name='initialview01'>1bkj</scene>, resolution 1.8&Aring;
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|SITE= <scene name='pdbsite=ASA:Fmn+Cofactor+Binding+Site-Chain+A'>ASA</scene> and <scene name='pdbsite=ASB:Fmn+Cofactor+Binding+Site-Chain+B'>ASB</scene>
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=FMN:FLAVIN MONONUCLEOTIDE'>FMN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_1.5.1.29 Transferred entry: 1.5.1.29], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.8.1 1.6.8.1]
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|GENE= VIBRIO HARVEYI NADPH\:FMN OXIDOREDUCTASE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=669 Vibrio harveyi])
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}}
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'''NADPH:FMN OXIDOREDUCTASE FROM VIBRIO HARVEYI'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1BKJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1CUM. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_1.5.1.29 Transferred entry: 1.5.1.29], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.8.1 1.6.8.1] Known structural/functional Sites: <scene name='pdbsite=ASA:Fmn+Cofactor+Binding+Site-Chain+A'>ASA</scene> and <scene name='pdbsite=ASB:Fmn+Cofactor+Binding+Site-Chain+B'>ASB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BKJ OCA].
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1BKJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi]. This structure supersedes the now removed PDB entry 1CUM. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BKJ OCA].
==Reference==
==Reference==
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Flavin reductase P: structure of a dimeric enzyme that reduces flavin., Tanner JJ, Lei B, Tu SC, Krause KL, Biochemistry. 1996 Oct 22;35(42):13531-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8885832 8885832]
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Flavin reductase P: structure of a dimeric enzyme that reduces flavin., Tanner JJ, Lei B, Tu SC, Krause KL, Biochemistry. 1996 Oct 22;35(42):13531-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8885832 8885832]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Transferred entry: 1 5.1 29]]
[[Category: Transferred entry: 1 5.1 29]]
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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 11:56:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:12:16 2008''

Revision as of 08:12, 20 March 2008

Image:1bkj.gif


PDB ID 1bkj

Drag the structure with the mouse to rotate
, resolution 1.8Å
Sites: and
Ligands: and
Gene: VIBRIO HARVEYI NADPH\:FMN OXIDOREDUCTASE (Vibrio harveyi)
Activity: Transferred entry: 1.5.1.29, with EC number 1.6.8.1
Coordinates: save as pdb, mmCIF, xml



NADPH:FMN OXIDOREDUCTASE FROM VIBRIO HARVEYI


Overview

We report the structure of an NADPH:FMN oxidoreductase (flavin reductase P) that is involved in bioluminescence by providing reduced FMN to luciferase. The 1.8 A crystal structure of flavin reductase P from Vibrio harveyi was solved by multiple isomorphous replacement and reveals that the enzyme is a unique dimer of interlocking subunits, with 9352 A2 of surface area buried in the dimer interface. Each subunit comprises two domains. The first domain consists of a four-stranded antiparallel beta-sheet flanked by helices on either side. The second domain reaches out from one subunit and embraces the other subunit and is responsible for interlocking the two subunits. Our structure explains why flavin reductase P is specific for FMN as cofactor. FMN is recognized and tightly bound by a network of 16 hydrogen bonds, while steric considerations prevent the binding of FAD. A flexible loop containing a Lys and an Arg could account for the NADPH specificity. The structure reveals information about several aspects of the catalytic mechanism. For example, we show that the first step in catalysis, which is hydride transfer from C4 of NADPH to cofactor FMN, involves addition to the re face of the FMN, probably at the N5 position. The limited accessibility of the FMN binding pocket and the extensive FMN-protein hydrogen bond network are consistent with the observed ping-pong bisubstrate--biproduct reaction kinetics. Finally, we propose a model for how flavin reductase P might shuttle electrons between NADPH and luciferase.

About this Structure

1BKJ is a Single protein structure of sequence from Vibrio harveyi. This structure supersedes the now removed PDB entry 1CUM. Full crystallographic information is available from OCA.

Reference

Flavin reductase P: structure of a dimeric enzyme that reduces flavin., Tanner JJ, Lei B, Tu SC, Krause KL, Biochemistry. 1996 Oct 22;35(42):13531-9. PMID:8885832

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