2V2K

THE CRYSTAL STRUCTURE OF FDXA, A 7FE FERREDOXIN FROM MYCOBACTERIUM SMEGMATIS

Summary for 2V2K

• Entry DOI: 10.2210/pdb2v2k/pdb
• Descriptor: FERREDOXIN, FE3-S4 CLUSTER, ACETATE ION, ... (4 entities in total)
• Functional Keywords: iron, transport, iron-sulfur, mycobacterium tuberculosis, fe-s cluster, metal-binding, 7fe ferredoxin, electron transfer, electron transport, mycobacterium smegmatis, 4fe-4s cluster instability
• Biological source: MYCOBACTERIUM SMEGMATIS
• Total number of polymer chains: 2
• Total formula weight: 24107.42

Authors

Ricagno, S.,de Rosa, M.,Aliverti, A.,Zanetti, G.,Bolognesi, M. (deposition date: 2007-06-06, release date: 2007-07-03, Last modification date: 2024-11-13)

Primary citation

Ricagno, S.,De Rosa, M.,Aliverti, A.,Zanetti, G.,Bolognesi, M.
The Crystal Structure of Fdxa, a 7Fe Ferredoxin from Mycobacterium Smegmatis.
Biochem.Biophys.Res.Commun., 360:97-, 2007

PubMed Abstract: Mycobacterium smegmatis ferredoxin FdxA, which has an orthologue ferredoxin in Mycobacterium tuberculosis, FdxC, contains both one [3Fe-4S] and one [4Fe-4S] cluster. M. smegmatis FdxA has been shown to be a preferred ferredoxin substrate of FprA [F. Fischer, D. Raimondi, A. Aliverti, G. Zanetti, Mycobacterium tuberculosis FprA, a novel bacterial NADPH-ferredoxin reductase, Eur. J. Biochem. 269 (2002) 3005-3013], an adrenodoxin reductase-like flavoprotein of M. tuberculosis, suggesting that M. tuberculosis FdxC could be the physiological partner of the enzyme in providing reducing power to the cytochromes P450. We report here the crystal structure of FdxA at 1.6A resolution (R(factor) 16.5%, R(free) 20.2%). Besides providing an insight on protein architecture for this 106-residue ferredoxin, our crystallographic investigation highlights lability of the [4Fe-4S] center, which is shown to loose a Fe atom during crystal growth. Due to their high similarity (87% sequence identity), the structure here reported can be considered a valuable model for M. tuberculosis FdxC, thus representing a step forward in the study of the complex mycobacterial redox pathways.

PubMed: 17577575
DOI: 10.1016/J.BBRC.2007.06.013

Experimental method

X-RAY DIFFRACTION (1.6 Å)