Structural highlights
Publication Abstract from PubMedMetallo-beta-lactamase (MBL) superfamily proteins have a common alphabeta/betaalpha sandwich fold and perform a variety of functions through metal-mediated catalysis. However, because of the enormous scale of this superfamily, only a small percentage of the proteins belonging to the superfamily have been annotated structurally or functionally to date. Therefore, much remains unknown about the MBL superfamily proteins. Here, TW9814, a hypothetical MBL superfamily protein, was structurally and functionally investigated. Guided by the crystal structure of dimeric TW9814, it was demonstrated that TW9814 functions as a phosphodiesterase (PDE) in the presence of divalent metal ions such as manganese(II) or nickel(II). A docking model between TW9814 and the substrate bis(p-nitrophenyl)phosphate (bpNPP) showed the importance of the dimerization of TW9814 for its bpNPP-hydrolyzing activity and for the interaction between the enzyme and the substrate. TW9814 showed outstanding catalytic efficiency (kcat/Km) under alkaline conditions compared with other PDEs. The activity of TW9814 appears to be regulated through a disulfide bond, which is a feature that is not present in other MBL superfamily members. This study provides a platform for the functional characterization of other hypothetical proteins of the MBL or other superfamilies. Structural and functional identification of the uncharacterized metallo-beta-lactamase superfamily protein TW9814 as a phosphodiesterase with unique metal coordination.,Heo Y, Park SB, Jeon YE, Yun JH, Jeong BG, Cha SS, Lee W Acta Crystallogr D Struct Biol. 2022 Apr 1;78(Pt 4):532-541. doi:, 10.1107/S2059798322002108. Epub 2022 Mar 17. PMID:35362475[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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