29PA

Helicobacter pylori glutamate racemase in complex with D-glutamate

Summary for 29PA

• Entry DOI: 10.2210/pdb29pa/pdb
• Descriptor: Glutamate racemase, D-GLUTAMIC ACID (3 entities in total)
• Functional Keywords: muri, d-glutamate, monoclinic symmetry, isomerase
• Biological source: Helicobacter pylori; More
• Total number of polymer chains: 2
• Total formula weight: 57358.64

Authors

Spiliopoulou, M.,Schulz, E.C. (deposition date: 2026-03-27, release date: 2026-10-28)

Primary citation

Spiliopoulou, M.,Schulz, E.C.
Structural analysis of Helicobacter pylori glutamate racemase in a monoclinic crystal form.
Acta Crystallogr.,Sect.F, 2026

PubMed Abstract: Glutamate racemase (MurI) catalyzes the stereochemical interconversion of L-glutamate and D-glutamate, a key element of bacterial peptidoglycan biosynthesis. In this study, we present the crystal structure of Helicobacter pylori glutamate racemase at 1.43 Å resolution and with monoclinic symmetry, as in previously reported models, but with different unit-cell parameters. The present model contains a single dimer in the asymmetric unit and retains the previously described head-to-head dimer arrangement. Comparative analysis of crystal packing reveals that the conserved dimeric assembly frequently adopts similar packing motifs, while differences in the relative arrangement of these dimeric arrays result in altered crystal packing and variations in unit-cell parameters. The monomeric fold and active-site architecture remain conserved and are consistent with the catalytic features described for bacterial glutamate racemases. This structure provides an updated, high-resolution structural model for H. pylori glutamate racemase and highlights the variability of crystal-packing arrangements within related monoclinic crystal forms.

PubMed: 42852900
DOI: 10.1107/S2053230X26008782

Experimental method

X-RAY DIFFRACTION (1.432 Å)