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X-ray crystal structure of Saccharomyces cerevisiae Pdx1 provides insights into the oligomeric nature of PLP synthases |
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| Authors: | Martina Neuwirth Marco Strohmeier Volker Windeisen Sigrid Deller Irmgard Sinning Ivo Tews |
| Institution: | a Technische Universität Graz, Institut für Biochemie, Petersgasse 12/2, A-8010 Graz, Austria b Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, 69120 Heidelberg, Germany c Deutsches Krebsforschungszentrum and BIOQUANT, Research Group Genome Organization & Function, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany |
| Abstract: | The universal enzymatic cofactor vitamin B6 can be synthesized as pyridoxal 5-phosphate (PLP) by the glutamine amidotransferase Pdx1. We show that Saccharomyces cerevisiae Pdx1 is hexameric by analytical ultracentrifugation and by crystallographic 3D structure determination. Bacterial homologues were previously reported to exist in hexamer:dodecamer equilibrium. A small sequence insertion found in yeast Pdx1 elevates the dodecamer dissociation constant when introduced into Bacillus subtilis Pdx1. Further, we demonstrate that the yeast Pdx1 C-terminus contacts an adjacent subunit, and deletion of this segment decreases enzymatic activity 3.5-fold, suggesting a role in catalysis.Structured summaryMINT-7147859: PDX1 (uniprotkb:P16451) and PDX1 (uniprotkb:P16451) bind (MI:0407) by cosedimentation in solution (MI:0028)MINT-7147899: PDX1 (uniprotkb:P37528) and PDX1 (uniprotkb:P37528) bind (MI:0407) by cosedimentation in solution (MI:0028) |
| Keywords: | BsPdx1 Pdx1 from Bacillus subtilis BsPdx1His6@K178 insertion mutant of BsPdx1 with a lysine residue in position 178 IPTG d-1-thiogalactopyranoside" target="_blank">isopropyl β-d-1-thiogalactopyranoside Kd dissociation constant MTG 1-thioglycerol PLP pyridoxal 5-phosphate ScPdx1 1 Pdx1 from Saccharomyces cerevisiae Tris 2-amino-2-(hydroxymethyl)-1 3-propanediol |
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