6K2L

Crystal structure of the Siderophore-interacting protein SipS from Aeromonas hydrophila

Summary for 6K2L

• Entry DOI: 10.2210/pdb6k2l/pdb
• Descriptor: Siderophore-interacting protein, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: siderophore-interacting protein, sips, aeromonas hydrophila, flavoprotein
• Biological source: Aeromonas hydrophila
• Total number of polymer chains: 2
• Total formula weight: 61509.20

Authors

Shang, F.,Lan, J.,Liu, W.,Xu, Y. (deposition date: 2019-05-14, release date: 2019-06-12, Last modification date: 2024-03-27)

Primary citation

Shang, F.,Lan, J.,Wang, L.,Liu, W.,Chen, Y.,Chen, J.,Ha, N.C.,Quan, C.,Nam, K.H.,Xu, Y.
Crystal structure of the Siderophore-interacting protein SIP from Aeromonas hydrophila.
Biochem.Biophys.Res.Commun., 519:23-28, 2019

PubMed Abstract: Siderophores acquire iron from hosts under iron-limiting conditions and play an essential role in the survival of microorganisms. Siderophore-interacting proteins (SIPs) from microbes release iron from the siderophore complex by reducing ferric iron to ferrous iron, but the molecular mechanism of iron reduction remains unclear. To better understand the molecular mechanism of SIPs, we herein report the crystal structure of Aeromonas hydrophila SIP (AhSIP) in complex with flavin adenine dinucleotide (FAD) as a cofactor. AhSIP consists of an N-terminal FAD binding domain and a C-terminal NADH binding domain, which are connected by a linker region. AhSIP showed unique structural differences in the orientation of the cofactor binding lobes when compared with SIP homologs. This study identified a cluster of three basic residues (Lys48, His259 and Arg262) in AhSIP distributed around a potential substrate binding pocket. In addition, AhSIP, containing the NADH binding motif E(L)VL-X-GE, belongs to the group I subfamily. Our results show the diverse cofactor and substrate binding sites of the SIP family.

PubMed: 31477273
DOI: 10.1016/j.bbrc.2019.08.085

Experimental method

X-RAY DIFFRACTION (2.5 Å)