6K2L

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

6K2L の概要

• エントリーDOI: 10.2210/pdb6k2l/pdb
• 分子名称: Siderophore-interacting protein, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: siderophore-interacting protein, sips, aeromonas hydrophila, flavoprotein
• 由来する生物種: Aeromonas hydrophila
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61509.20

構造登録者

Shang, F.,Lan, J.,Liu, W.,Xu, Y. (登録日: 2019-05-14, 公開日: 2019-06-12, 最終更新日: 2024-03-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)