2v5v
From Proteopedia
Line 1: | Line 1: | ||
[[Image:2v5v.gif|left|200px]] | [[Image:2v5v.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_2v5v", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | + | --> | |
- | | | + | {{STRUCTURE_2v5v| PDB=2v5v | SCENE= }} |
- | | | + | |
- | + | ||
- | }} | + | |
'''W57E FLAVODOXIN FROM ANABAENA''' | '''W57E FLAVODOXIN FROM ANABAENA''' | ||
Line 31: | Line 28: | ||
[[Category: Medina, M.]] | [[Category: Medina, M.]] | ||
[[Category: Perez-Dorado, I.]] | [[Category: Perez-Dorado, I.]] | ||
- | [[Category: | + | [[Category: Electron transfer]] |
- | [[Category: | + | [[Category: Electron transport]] |
- | [[Category: | + | [[Category: Flavoprotein]] |
- | [[Category: | + | [[Category: Fmn]] |
- | [[Category: | + | [[Category: Transport]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:13:52 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 15:13, 4 May 2008
W57E FLAVODOXIN FROM ANABAENA
Overview
Contribution of three regions (phosphate-binding, 50's and 90's loops) of Anabaena apoflavodoxin to FMN binding and reduction potential was studied. Thr12 and Glu16 did not influence FMN redox properties, but Thr12 played a role in FMN binding. Replacement of Trp57 with Glu, Lys or Arg moderately shifted E(ox/sq) and E(sq/hq) and altered the energetic of the FMN redox states binding profile. Our data indicate that the side chain of position 57 does not modulate E(ox/sq) by aromatic stacking or solvent exclusion, but rather by influencing the relative strength of the H-bond between the N(5) of the flavin and the Asn58-Ile59 bond. A correlation was observed between the isoalloxazine increase in solvent accessibility and less negative E(sq/hq). Moreover, E(sq/hq) became less negative as positively charged residues were added near to the isoalloxazine. Ile59 and Ile92 were simultaneously mutated to Ala or Glu. These mutations impaired FMN binding, while shifting E(sq/hq) to less negative values and E(ox/sq) to more negative. These effects are discussed on the bases of the X-ray structures of some of the Fld mutants, suggesting that in Anabaena Fld the structural control of both electron transfer steps is much more subtle than in other Flds.
About this Structure
2V5V is a Single protein structure of sequence from Anabaena sp.. Full crystallographic information is available from OCA.
Reference
Tuning of the FMN binding and oxido-reduction properties by neighboring side chains in Anabaena flavodoxin., Frago S, Goni G, Herguedas B, Peregrina JR, Serrano A, Perez-Dorado I, Molina R, Gomez-Moreno C, Hermoso JA, Martinez-Julvez M, Mayhew SG, Medina M, Arch Biochem Biophys. 2007 Nov 15;467(2):206-17. Epub 2007 Aug 29. PMID:17904516 Page seeded by OCA on Sun May 4 18:13:52 2008