7LXG

Homocitrullinated beta-lactamase OXA-48

Summary for 7LXG

• Entry DOI: 10.2210/pdb7lxg/pdb
• Descriptor: Beta-lactamase, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: homocitrulline, oxa-48, beta-lactamase, hydrolase
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 2
• Total formula weight: 64722.96

Authors

Serrano-Negron, J.E.,King, D.T.,Vocadlo, D.J. (deposition date: 2021-03-03, release date: 2022-05-25, Last modification date: 2023-10-18)

Primary citation

King, D.T.,Zhu, S.,Hardie, D.B.,Serrano-Negron, J.E.,Madden, Z.,Kolappan, S.,Vocadlo, D.J.
Chemoproteomic identification of CO 2 -dependent lysine carboxylation in proteins.
Nat.Chem.Biol., 18:782-791, 2022

PubMed Abstract: Carbon dioxide is an omnipresent gas that drives adaptive responses within organisms from all domains of life. The molecular mechanisms by which proteins serve as sensors of CO are, accordingly, of great interest. Because CO is electrophilic, one way it can modulate protein biochemistry is by carboxylation of the amine group of lysine residues. However, the resulting CO-carboxylated lysines spontaneously decompose, giving off CO, which makes studying this modification difficult. Here we describe a method to stably mimic CO-carboxylated lysine residues in proteins. We leverage this method to develop a quantitative approach to identify CO-carboxylated lysines of proteins and explore the lysine 'carboxylome' of the CO-responsive cyanobacterium Synechocystis sp. We uncover one CO-carboxylated lysine within the effector binding pocket of the metabolic signaling protein PII. CO-carboxylatation of this lysine markedly lowers the affinity of PII for its regulatory effector ligand ATP, illuminating a negative molecular control mechanism mediated by CO.

PubMed: 35710617
DOI: 10.1038/s41589-022-01043-1

Experimental method

X-RAY DIFFRACTION (2.2 Å)