6x0b
Crystal Structure of Thioredoxin NaTrxh from Nicotiana alataCrystal Structure of Thioredoxin NaTrxh from Nicotiana alata
Structural highlights
FunctionPublication Abstract from PubMedThioredoxins are regulatory proteins that reduce disulfide bonds on target proteins. NaTrxh, which belongs to the plant thioredoxin family h subgroup 2, interacts and reduces the S-RNase enhancing its ribonuclease activity seven-fold, resulting an essential protein for pollen rejection inNicotiana.Here, the crystal structure of NaTrxh at 1.7 A by X-ray diffraction is reported. NaTrxh conserves the typical fold observed in other thioredoxins from prokaryotes and eukaryotes, but it contains extensions towards both N- and C-termini.The NaTrxh N-terminal extension participates in the reduction of S-RNase, and in the structure reported here, this is orientated towards the reactive site. The interaction between SF11-RNase and the NaTrxh N-terminal was simulated and the short-lived complex observed lasted for a tenth of ns. Moreover, we identified certain amino acids as SF11-RNase-E155 and NaTrxh-M104 as good candidates to contribute to the stability of the complex. Furthermore, we simulated the reduction of the C153-C186 SF11-RNase disulfide bond and observed subtle changes that affect the entire core, which might explain the increase in the ribonuclease activity of S-RNase when it is reduced by NaTrxh. High resolution crystal structure of NaTrxh from Nicotiana alata and its interaction with the S-RNase.,Maria Daniela TR, Lilian GS, Rogelio RS, Javier Andres JD, Yuridia CZ, Felipe CG J Struct Biol. 2020 Jul 16:107578. doi: 10.1016/j.jsb.2020.107578. PMID:32682729[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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