4jax | pdb_00004jax

Crystal structure of dimeric KlHxk1 in crystal form X

spinqualitylabelsall models 4jax, resolution 2.26Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4jax is a 6 chain structure with sequence from Kluyveromyces lactis NRRL Y-1140. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.26Å Ligands: GOL, PO4, SEP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HXK_KLULA Publication Abstract from PubMed The bifunctional hexokinase KlHxk1 is a key component of glucose dependent signal transduction in Kluyveromyces lactis. KlHxk1 is phosphorylated in vivo and undergoes ATP-dependent autophosphorylation-inactivation in vitro. This study identifies serine-15 as the site of in vivo phosphorylation and serine-157 as the autophosphorylation-inactivation site. X-ray crystallography of the in vivo phosphorylated enzyme indicates the existence of a ring-shaped symmetrical homodimer carrying two phosphoserine-15 residues. In contrast, small-angle X-ray scattering and equilibrium sedimentation analyses reveal the existence of monomeric phosphoserine-15 KlHxk1 in solution. While phosphorylation at serine-15 and concomitant homodimer dissociation are likely to be involved in glucose signalling, mechanism and putative physiological significance of KlHxk1 inactivation by autophosphorylation at serine-157 remain to be established. In vivo phosphorylation and in vitro autophosphorylation-inactivation of Kluyveromyces lactis hexokinase KlHxk1.,Kettner K, Kuettner EB, Otto A, Lilie H, Golbik RP, Strater N, Kriegel TM Biochem Biophys Res Commun. 2013 Apr 10. pii: S0006-291X(13)00600-1. doi:, 10.1016/j.bbrc.2013.03.121. PMID:23583397 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hexokinase 3D structures

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