1akw: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /> <applet load="1akw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1akw, resolution 1.75Å" /> '''G61L OXIDIZED FLAVO...
 
No edit summary
Line 8: Line 8:


==About this Structure==
==About this Structure==
1AKW is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]] with FMN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AKW OCA]].  
1AKW is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]] with FMN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: FMN. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AKW OCA]].  


==Reference==
==Reference==
Line 25: Line 25:
[[Category: mutant]]
[[Category: mutant]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:25:43 2007''
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:33:28 2007''

Revision as of 13:28, 30 October 2007

File:1akw.gif


1akw, resolution 1.75Å

Drag the structure with the mouse to rotate

G61L OXIDIZED FLAVODOXIN MUTANT

OverviewOverview

Mutants of the electron-transfer protein flavodoxin from Desulfovibrio, vulgaris were made by site-directed mutagenesis to investigate the role of, glycine-61 in stabilizing the semiquinone of FMN by the protein and in, controlling the flavin redox potentials. The spectroscopic properties, oxidation-reduction potentials, and flavin-binding properties of the, mutant proteins, G61A/N/V and L, were compared with those of wild-type, flavodoxin. The affinities of all of the mutant apoproteins for FMN and, riboflavin were less than that of the wild-type apoprotein, and the redox, potentials of the two 1-electron steps in the reduction of the complex, with FMN were also affected by the mutations. Values for the dissociation, constants of the complexes of the apoprotein with the semiquinone and, ... [(full description)]

About this StructureAbout this Structure

1AKW is a [Single protein] structure of sequence from [Desulfovibrio vulgaris] with FMN as [ligand]. Structure known Active Site: FMN. Full crystallographic information is available from [OCA].

ReferenceReference

Modulation of the redox potentials of FMN in Desulfovibrio vulgaris flavodoxin: thermodynamic properties and crystal structures of glycine-61 mutants., O'Farrell PA, Walsh MA, McCarthy AA, Higgins TM, Voordouw G, Mayhew SG, Biochemistry. 1998 Jun 9;37(23):8405-16. PMID:9622492

Page seeded by OCA on Tue Oct 30 12:33:28 2007

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA