Crystal structure of a putative short-chain dehydrogenase/reductase from Paraburkholderia xenovorans
Jayson Davidson, Kyndall Nicholas, Jeremy Young, Deborah G. Conrady, Stephen Mayclin, Sandhya Subramanian, Bart L. Staker, Peter J. Myler and Oluwatoyin A. Asojo [1]
Molecular Tour
The high-resolution structure of a putative short-chain reductase from the commercially important bacteria Paraburkholderia xenovorans is reported (PxSDR). P. xenovorans degrades organic wastes like polychlorinated biphenyls. PxSDR shares less than 37% sequence identity with any known structure and assembles as a prototypical SDR tetramer. As expected, there is some conformational flexibility and differences between the substrate-binding cavity, which explains substrate specificity. Uniquely, the cofactor binding cavity of PxSDR is not well conserved and differs from other SDRs. PxSDR has an additional seven-amino acids that form an additional unique loop within the co-factor binding cavity. Further studies are required to determine how these differences affect the enzymatic functions of the SDR. This project is an educational collaboration between the Seattle Structural Genomics Center for Infectious Disease (SSGCID) and Hampton University where undergraduate students are engaged in structure-function analysis and publication of structures solved by the SSGCID.
References
- ↑ Davidson J, Nicholas K, Young J, Conrady DG, Mayclin S, Subramanian S, Staker BL, Myler PJ, Asojo OA. Crystal structure of a putative short-chain dehydrogenase/reductase from Paraburkholderia xenovorans. Acta Crystallogr F Struct Biol Commun. 2022 Jan 1;78(Pt 1):25-30. doi:, 10.1107/S2053230X21012632. Epub 2022 Jan 1. PMID:34981772 doi:http://dx.doi.org/10.1107/S2053230X21012632
