3ESX

E16KE61KD126KD150K Flavodoxin from Anabaena

Summary for 3ESX

• Entry DOI: 10.2210/pdb3esx/pdb
• Related: 3ESY 3ESZ
• Descriptor: Flavodoxin, FLAVIN MONONUCLEOTIDE, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: alpha and beta protein, electron transport, flavoprotein, fmn, transport
• Biological source: Anabaena sp.
• Total number of polymer chains: 2
• Total formula weight: 38820.07

Authors

Herguedas, B.,Hermoso, J.A.,Martinez-Julvez, M.,Goni, G.,Medina, M. (deposition date: 2008-10-06, release date: 2009-02-10, Last modification date: 2023-11-01)

Primary citation

Goni, G.,Herguedas, B.,Hervas, M.,Peregrina, J.R.,De la Rosa, M.A.,Gomez-Moreno, C.,Navarro, J.A.,Hermoso, J.A.,Martinez-Julvez, M.,Medina, M.
Flavodoxin: A compromise between efficiency and versatility in the electron transfer from Photosystem I to Ferredoxin-NADP(+) reductase
Biochim.Biophys.Acta, 1787:144-154, 2009

PubMed Abstract: Under iron-deficient conditions Flavodoxin (Fld) replaces Ferredoxin in Anabaena as electron carrier from Photosystem I (PSI) to Ferredoxin-NADP(+) reductase (FNR). Several residues modulate the Fld interaction with FNR and PSI, but no one appears as specifically critical for efficient electron transfer (ET). Fld shows a strong dipole moment, with its negative end directed towards the flavin ring. The role of this dipole moment in the processes of interaction and ET with positively charged surfaces exhibited by PSI and FNR has been analysed by introducing single and multiple charge reversal mutations on the Fld surface. Our data confirm that in this system interactions do not rely on a precise complementary surface of the reacting molecules. In fact, they indicate that the initial orientation driven by the alignment of dipole moment of the Fld molecule with that of the partner contributes to the formation of a bunch of alternative binding modes competent for the efficient ET reaction. Additionally, the fact that Fld uses different interaction surfaces to dock to PSI and to FNR is confirmed.

PubMed: 19150326
DOI: 10.1016/j.bbabio.2008.12.006

Experimental method

X-RAY DIFFRACTION (2.31 Å)