This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1vfr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vfr.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1vfr.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1vfr| PDB=1vfr | SCENE= }}
{{STRUCTURE_1vfr| PDB=1vfr | SCENE= }}
-
'''THE MAJOR NAD(P)H:FMN OXIDOREDUCTASE FROM VIBRIO FISCHERI'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9654450}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9654450 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9654450}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Vibrio fischeri]]
[[Category: Vibrio fischeri]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:29:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:11:14 2008''

Revision as of 05:11, 29 July 2008

Image:1vfr.png

Template:STRUCTURE 1vfr

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

Template:ABSTRACT PUBMED 9654450

About this Structure

1VFR is a Single protein structure of sequence from Aliivibrio fischeri. 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

Page seeded by OCA on Tue Jul 29 08:11:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vfr"
Personal tools