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Crystal Structure of Aeromonas hydrophila Cytoplasmic 5 '-Methylthioadenosine/S-Adenosylhomocysteine Nucleosidase

Authors
Chen, JinliLiu, WeiWang, LuluShang, FeiChen, YuanyuanLan, JingGao, PengHa, Nam-ChulQuan, ChunshanNam, Ki HyunXu, Yongbin
Issue Date
23-7월-2019
Publisher
AMER CHEMICAL SOC
Citation
BIOCHEMISTRY, v.58, no.29, pp.3136 - 3143
Indexed
SCIE
SCOPUS
Journal Title
BIOCHEMISTRY
Volume
58
Number
29
Start Page
3136
End Page
3143
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/64073
DOI
10.1021/acs.biochem.9b00174
ISSN
0006-2960
Abstract
5'-Methylthioadenosine/S-adenosyl-L-homocysteine (MTA/SAH) nucleosidase (MTAN) is an important enzyme in a number of critical biological processes. Mammals do not express MtaN, making this enzyme an attractive antibacterial drug target. In pathogen Aeromonas hydrophila, two MtnN subfamily genes (MtaN-1 and MtaN-2) play important roles in the periplasm and cytosol, respectively. We previously reported structural and functional analyses of MtaN-1, but little is known regarding MtaN-2 due to the lack of a crystal structure. Here, we determined the crystal structure of cytosolic A. hydrophila MtaN-2 in complex with adenine (ADE), which is a cleavage product of adenosine. AhMtaN-1 and AhMtaN-2 exhibit a high degree of similarity in the alpha-beta-alpha sandwich fold of the core structural motif. However, there is a structural difference in the nonconserved extended loop between beta 7 and alpha 3 that is associated with the channel depth of the substrate-binding pocket and dimerization. The ADE molecules in the substrate-binding pockets of AhMtaN-1 and AhMtaN-2 are stabilized with pi-pi stacking by Trp199 and Phe152, respectively, and the hydrophobic residues surrounding the ribose-binding sites differ. A structural comparison of AhMtaN-2 with other MtaN proteins showed that MtnN subfamily proteins exhibit a unique substrate-binding surface and dimerization interface.
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