Crystal structure of the polyketide cyclase from Mycobacterium tuberculosis  

作　　者：Jie Zhuang Shihui Fan Chenyun Guo Liubin Feng Huilin Wang Donghai Lin Xinli Liao 

机构地区：[1]Department of Chemistry,College of Chemistry and Chemical Engineering,Xiamen University,Xiamen 361005,China [2]Department of Chemical Biology,College of Chemistry and Chemical Engineering,Xiamen University,Xiamen 361005,China

出　　处：《Acta Biochimica et Biophysica Sinica》2022年第4期474-481,共8页生物化学与生物物理学报（英文版）

基　　金：the grants from the National Key Research and Development Project of China(No.2016YFA0500600)。

摘　　要：About 40%of proteins are classified as conserved hypothetical proteins in Mycobacterium tuberculosis(TB).Identification and characterization of these proteins are beneficial to understand the pathogenesis of TB and exploiting novel drugs for TB treatments.The polyketide cyclase,a protein from M.tuberculosis(MtPC)has been annotated as a hypothetical protein in Uniprot database.Sequence analysis shows that the MtPC belongs to the NTF2-like superfamily proteins with diverse functions.Here,we determined the crystal structure of MtPC at a resolution of 2.4Åand measured backbone relaxation parameters for the MtPC protein.MtPC exists as a dimer in solution,and each subunit contains a six-stranded mixedβ-sheet and threeαhelixes which are arranged in the orderα1-α2-β1-β2-α3-β3-β4-β5-β6.The NMR dynamics analysis showed that the overall structure of MtPC is highly rigid on ps-ns time scales.Furthermore,we predicted the potential function of MtPC based on the crystal structure.Our results lay the basis for further exploiting and mechanistically understanding the biological functions of MtPC.

关 键 词：MtPC crystal structure Mycobacterium tuberculosis NMR dynamics NTF2-like superfamily protein 

分 类 号：R52[医药卫生—内科学]