6UTT

LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase in complex with calcium

Summary for 6UTT

• Entry DOI: 10.2210/pdb6utt/pdb
• Descriptor: ATP-dependent sacrificial sulfur transferase LarE, PHOSPHATE ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: lar, sulfur transferase, lare, ampylation, pp-loop, atp pyrophophatase domain, lactate racemization, lactate racemase, transferase
• Biological source: Lactobacillus plantarum
• Total number of polymer chains: 6
• Total formula weight: 191538.96

Authors

Fellner, M.,Huizenga, K.,Hausinger, R.P.,Hu, J. (deposition date: 2019-10-29, release date: 2019-11-06, Last modification date: 2023-10-11)

Primary citation

Fellner, M.,Huizenga, K.G.,Hausinger, R.P.,Hu, J.
Crystallographic characterization of a tri-Asp metal-binding site at the three-fold symmetry axis of LarE.
Sci Rep, 10:5830-5830, 2020

PubMed Abstract: Detailed crystallographic characterization of a tri-aspartate metal-binding site previously identified on the three-fold symmetry axis of a hexameric enzyme, LarE from Lactobacillus plantarum, was conducted. By screening an array of monovalent, divalent, and trivalent metal ions, we demonstrated that this metal binding site stoichiometrically binds Ca, Mn, Fe/Fe, Co, Ni, Cu, Zn, and Cd, but not monovalent metal ions, Cr, Mg, Y, Sr or Ba. Extensive database searches resulted in only 13 similar metal binding sites in other proteins, indicative of the rareness of tri-aspartate architectures, which allows for engineering such a selective multivalent metal ion binding site into target macromolecules for structural and biophysical characterization.

PubMed: 32242052
DOI: 10.1038/s41598-020-62847-6

Experimental method

X-RAY DIFFRACTION (2.49 Å)