6K2Q

Aeromonas hydrophila MtaN-2 complexed with adenine

Summary for 6K2Q

• Entry DOI: 10.2210/pdb6k2q/pdb
• Descriptor: 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase, ADENINE (3 entities in total)
• Functional Keywords: aeromonas hydrophila, mtan-2, complex, adenine, 5'-methylthioadenosine/s-adenosylhomocysteine nucleosidase, hydrolase
• Biological source: eromonas hydrophila subsp. hydrophila ATCC 7966
• Total number of polymer chains: 4
• Total formula weight: 113542.35

Authors

Chen, J.,Liu, W.,Wang, L.,Shang, F.,Lan, J.,Chen, Y.,Xu, Y. (deposition date: 2019-05-15, release date: 2019-05-29, Last modification date: 2023-11-22)

Primary citation

Chen, J.,Liu, W.,Wang, L.,Shang, F.,Chen, Y.,Lan, J.,Gao, P.,Ha, N.C.,Quan, C.,Nam, K.H.,Xu, Y.
Crystal Structure of Aeromonas hydrophila Cytoplasmic 5'-Methylthioadenosine/S-Adenosylhomocysteine Nucleosidase.
Biochemistry, 58:3136-3143, 2019

PubMed Abstract: 5'-Methylthioadenosine/-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 , 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 MtaN-2 in complex with adenine (ADE), which is a cleavage product of adenosine. MtaN-1 and MtaN-2 exhibit a high degree of similarity in the α-β-α sandwich fold of the core structural motif. However, there is a structural difference in the nonconserved extended loop between β7 and α3 that is associated with the channel depth of the substrate-binding pocket and dimerization. The ADE molecules in the substrate-binding pockets of MtaN-1 and MtaN-2 are stabilized with π-π stacking by Trp199 and Phe152, respectively, and the hydrophobic residues surrounding the ribose-binding sites differ. A structural comparison of MtaN-2 with other MtaN proteins showed that MtnN subfamily proteins exhibit a unique substrate-binding surface and dimerization interface.

PubMed: 31274299
DOI: 10.1021/acs.biochem.9b00174

Experimental method

X-RAY DIFFRACTION (2 Å)