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The X-ray structure of juvenile hormone diol kinase from the silkworm Bombyx mori

DOI: 10.1107/S2053230X21012012 DOI Help

Authors: Jingxu Guo (University College London; University of Cambridge) , Ronan M. Keegan (Science and Technologies Facilities Council) , Daniel J. Rigden (University of Liverpool) , Peter T. Erskine (University College London; Birkbeck, University of London) , Steve P. Wood (University College London; University of Portsmouth) , Sheng Li (Shanghai Institutes for Biological Sciences) , Jonathan B. Cooper (University College London; Birkbeck, University of London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 77

State: Published (Approved)
Published: December 2021
Diamond Proposal Number(s): 12342

Abstract: Insect juvenile hormones (JHs) are a family of sesquiterpenoid molecules that are secreted into the haemolymph. JHs have multiple roles in insect development, metamorphosis and sexual maturation. A number of pesticides work by chemically mimicking JHs, thus preventing insects from developing and reproducing normally. The haemolymph levels of JH are governed by the rates of its biosynthesis and degradation. One enzyme involved in JH catabolism is JH diol kinase (JHDK), which uses ATP (or GTP) to phosphorylate JH diol to JH diol phosphate, which can be excreted. The X-ray structure of JHDK from the silkworm Bombyx mori has been determined at a resolution of 2.0 Å with an R factor of 19.0% and an Rfree of 24.8%. The structure possesses three EF-hand motifs which are occupied by calcium ions. This is in contrast to the recently reported structure of the JHDK-like-2 protein from B. mori (PDB entry 6kth), which possessed only one calcium ion. Since JHDK is known to be inhibited by calcium ions, it is likely that our structure represents the calcium-inhibited form of the enzyme. The electrostatic surface of the protein suggests a binding site for the triphosphate of ATP close to the N-terminal end of the molecule in a cavity between the N- and C-terminal domains. Superposition with a number of calcium-activated photoproteins suggests that there may be parallels between the binding of JH diol to JHDK and the binding of luciferin to aequorin.

Journal Keywords: kinases; EF-hand motifs; molecular replacement; insect juvenile hormones; metamorphosis; Bombyx mori

Diamond Keywords: Enzymes

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography

Added On: 26/11/2021 10:42

Discipline Tags:

Genetics Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)