4jax: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jax]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis_NRRL_Y-1140 Kluyveromyces lactis NRRL Y-1140]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JAX FirstGlance]. <br> | <table><tr><td colspan='2'>[[4jax]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis_NRRL_Y-1140 Kluyveromyces lactis NRRL Y-1140]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JAX FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jax OCA], [https://pdbe.org/4jax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jax RCSB], [https://www.ebi.ac.uk/pdbsum/4jax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jax ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jax OCA], [https://pdbe.org/4jax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jax RCSB], [https://www.ebi.ac.uk/pdbsum/4jax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jax ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 18:39, 20 September 2023
Crystal structure of dimeric KlHxk1 in crystal form XCrystal structure of dimeric KlHxk1 in crystal form X
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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