1vfr
From Proteopedia
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==Overview== | ==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 ... | + | 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 (NOX) in spite, of the very low identity in amino acid sequences (10% with FRP and 21%, with NOX). 56% of alpha-carbons of FRase I core residues could be, superposed onto NOX counterparts with an r.m.s. distance of 1.2 A. The, remaining residues have relatively high B-values and may be essential for, defining the substrate specificity. Indeed, one of them, Phe124, was found, to participate in the binding of dicoumarol through stacking to one of the, rings of dicoumarol. Upon binding of dicoumarol, most of the exposed, re-face of the FMN cofactor is buried, which is consistent with the ping, pong bi bi catalytic mechanism. |
==About this Structure== | ==About this Structure== | ||
| - | 1VFR is a | + | 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== | ||
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[[Category: vibrio fischeri]] | [[Category: vibrio fischeri]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:54:07 2007'' |
Revision as of 10:48, 5 November 2007
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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 (NOX) in spite, of the very low identity in amino acid sequences (10% with FRP and 21%, with NOX). 56% of alpha-carbons of FRase I core residues could be, superposed onto NOX counterparts with an r.m.s. distance of 1.2 A. The, remaining residues have relatively high B-values and may be essential for, defining the substrate specificity. Indeed, one of them, Phe124, was found, to participate in the binding of dicoumarol through stacking to one of the, rings of dicoumarol. Upon binding of dicoumarol, most of the exposed, re-face of the FMN cofactor is buried, which is consistent with the ping, pong bi bi catalytic mechanism.
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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