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1vfr

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(New page: 200px<br /> <applet load="1vfr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vfr, resolution 1.8&Aring;" /> '''THE MAJOR NAD(P)H:FM...)
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==About this Structure==
==About this Structure==
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1VFR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Vibrio_fischeri Vibrio fischeri]] with FMN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.8.1 1.6.8.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VFR OCA]].
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1VFR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Vibrio_fischeri Vibrio fischeri]] with FMN as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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]]. Structure known Active Sites: FM2 and FMN. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VFR OCA]].
==Reference==
==Reference==
1.8 A crystal structure of the major NAD(P)H:FMN oxidoreductase of a bioluminescent bacterium, Vibrio fischeri: overall structure, cofactor and substrate-analog binding, and comparison with related flavoproteins., Koike H, Sasaki H, Kobori T, Zenno S, Saigo K, Murphy ME, Adman ET, Tanokura M, J Mol Biol. 1998 Jul 10;280(2):259-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9654450 9654450]
1.8 A crystal structure of the major NAD(P)H:FMN oxidoreductase of a bioluminescent bacterium, Vibrio fischeri: overall structure, cofactor and substrate-analog binding, and comparison with related flavoproteins., Koike H, Sasaki H, Kobori T, Zenno S, Saigo K, Murphy ME, Adman ET, Tanokura M, J Mol Biol. 1998 Jul 10;280(2):259-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9654450 9654450]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Transferred entry: 1.5.1.29]]
[[Category: Vibrio fischeri]]
[[Category: Vibrio fischeri]]
[[Category: Adman, E.T.]]
[[Category: Adman, E.T.]]
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[[Category: vibrio fischeri]]
[[Category: vibrio fischeri]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:02:51 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:57:49 2007''

Revision as of 08:53, 30 October 2007


1vfr, resolution 1.8Å

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THE MAJOR NAD(P)H:FMN OXIDOREDUCTASE FROM VIBRIO FISCHERI

Overview

We have solved the crystal structure of FRase I, the major NAD(P)H:FMN, oxidoreductase of Vibrio fischeri, by the multiple isomorphous replacement, method (MIR) at 1.8 A resolution with the conventional R factor of 0.187., The crystal structure of FRase I complexed with its competitive inhibitor, dicoumarol, has also been solved at 2.2 A resolution with the conventional, R factor of 0.161. FRase I is a homodimer, having one FMN cofactor per, subunit, which is situated at the interface of two subunits. The overall, fold can be divided into two domains; 80% of the residues form a rigid, core and the remaining, a small flexible domain. The overall core folding, is similar to those of an NADPH-dependent flavin reductase of Vibrio, harveyi (FRP) and the NADH oxidase of Thermus thermophilus ... [(full description)]

About this Structure

1VFR is a [Single protein] structure of sequence from [Vibrio fischeri] with FMN as [ligand]. Active as [Transferred entry: 1.5.1.29], with EC number [1.6.8.1]. Structure known Active Sites: FM2 and FMN. Full crystallographic information is available from [OCA].

Reference

1.8 A crystal structure of the major NAD(P)H:FMN oxidoreductase of a bioluminescent bacterium, Vibrio fischeri: overall structure, cofactor and substrate-analog binding, and comparison with related flavoproteins., Koike H, Sasaki H, Kobori T, Zenno S, Saigo K, Murphy ME, Adman ET, Tanokura M, J Mol Biol. 1998 Jul 10;280(2):259-73. PMID:9654450

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