6k2q

Aeromonas hydrophila MtaN-2 complexed with adenine

spinqualitylabelsall models 6k2q, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6k2q is a 4 chain structure with sequence from Aeromonas hydrophila subsp. hydrophila ATCC 7966. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: ADE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MTNN_AERHH Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Publication Abstract from PubMed 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 beta7 and alpha3 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. Crystal Structure of Aeromonas hydrophila Cytoplasmic 5'-Methylthioadenosine/S-Adenosylhomocysteine Nucleosidase.,Chen J, Liu W, Wang L, Shang F, Chen Y, Lan J, Gao P, Ha NC, Quan C, Nam KH, Xu Y Biochemistry. 2019 Jul 23;58(29):3136-3143. doi: 10.1021/acs.biochem.9b00174., Epub 2019 Jul 10. PMID:31274299 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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