3FEM

Structure of the synthase subunit Pdx1.1 (Snz1) of PLP synthase from Saccharomyces cerevisiae

Summary for 3FEM

• Entry DOI: 10.2210/pdb3fem/pdb
• Related: 1ZNN 2ISS 2NV1 2NV2
• Descriptor: Pyridoxine biosynthesis protein SNZ1 (2 entities in total)
• Functional Keywords: (beta/alpha)8-barrel, synthase, pyridoxine biosynthesis, biosynthetic protein, transferase
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Total number of polymer chains: 6
• Total formula weight: 191147.32

Authors

Strohmeier, M.,Windeisen, V.,Sinning, I.,Tews, I. (deposition date: 2008-11-30, release date: 2009-06-16, Last modification date: 2023-11-01)

Primary citation

Neuwirth, M.,Strohmeier, M.,Windeisen, V.,Wallner, S.,Deller, S.,Rippe, K.,Sinning, I.,Macheroux, P.,Tews, I.
X-ray crystal structure of Saccharomyces cerevisiae Pdx1 provides insights into the oligomeric nature of PLP synthases.
Febs Lett., 583:2179-2186, 2009

PubMed 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.

PubMed: 19523954
DOI: 10.1016/j.febslet.2009.06.009

Experimental method

X-RAY DIFFRACTION (3.02 Å)