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6KTH

Crystal structure of Juvenile hormone diol kinase JHDK-L2 from silkworm, Bombyx mori

Summary for 6KTH
Entry DOI10.2210/pdb6kth/pdb
DescriptorJuvenile hormone diol kinase, CALCIUM ION, GLYCEROL, ... (4 entities in total)
Functional Keywordskinase, catabolism, ef-hand motif, hormone
Biological sourceBombyx mori (Silk moth)
Total number of polymer chains1
Total formula weight22829.02
Authors
Zhang, Y.S.,Xu, H.Y.,Wang, Z.,Zhang, L.,Zhao, P.,Guo, P.C. (deposition date: 2019-08-28, release date: 2020-09-02, Last modification date: 2023-11-22)
Primary citationXu, H.,Zhang, Y.,Zhang, L.,Wang, Z.,Guo, P.,Zhao, P.
Structural characterization and functional analysis of juvenile hormone diol kinase from the silkworm, Bombyx mori.
Int.J.Biol.Macromol., 167:570-577, 2021
Cited by
PubMed Abstract: Juvenile hormone diol kinase (JHDK) is an important enzyme involved in the juvenile hormone metabolism pathway, which catalyzes the phosphorylation of juvenile hormone diol to form the polar metabolite JH diol phosphate. Here, we reported the first crystal structure of insect JHDK from Bombyx mori, BmJHDK-L2, determined at a resolution of 1.22 Å. The structure of BmJHDK-L2 mainly comprises of eight α-helical segments linked with loops, forming four helix-loop-helix motifs. In these four helix-loop-helix motifs with only one calcium ion bound in the first motif. Circular dichroism spectra indicated that BmJHDK-L2 has strong thermal stability, which is independent of the divalent cation. The structure of BmJHDK-L2 further allowed us to define an ATP-binding site using computational simulation and binding assays, providing a structural basis for development of inhibitor of JHDK. Moreover, the expression profile of BmJHDK-L2 indicated a predominant role in juvenile hormone metabolism in the Malpighian tubules of silkworm. Collectively, these findings expand our knowledge regarding the structural and biochemical features of insect JHDK proteins.
PubMed: 33249150
DOI: 10.1016/j.ijbiomac.2020.11.138
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.22 Å)
Structure validation

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