4QEC

ElxO with NADP Bound

Summary for 4QEC

• Entry DOI: 10.2210/pdb4qec/pdb
• Related: 4QED
• Descriptor: ElxO, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: rossmann fold, oxidoreductase
• Biological source: Staphylococcus epidermidis
• Total number of polymer chains: 2
• Total formula weight: 56673.91

Authors

Garg, N.,Nair, S.K. (deposition date: 2014-05-15, release date: 2014-07-02, Last modification date: 2024-02-28)

Primary citation

Ortega, M.A.,Velasquez, J.E.,Garg, N.,Zhang, Q.,Joyce, R.E.,Nair, S.K.,van der Donk, W.A.
Substrate Specificity of the Lanthipeptide Peptidase ElxP and the Oxidoreductase ElxO.
Acs Chem.Biol., 9:1718-1725, 2014

PubMed Abstract: The final step in lanthipeptide biosynthesis involves the proteolytic removal of an N-terminal leader peptide. In the class I lanthipeptide epilancin 15X, this step is performed by the subtilisin-like serine peptidase ElxP. Bioinformatic, kinetic, and mass spectrometric analysis revealed that ElxP recognizes the stretch of amino acids DLNPQS located near the proteolytic cleavage site of its substrate, ElxA. When the ElxP recognition motif was inserted into the noncognate lanthipeptide precursor NisA, ElxP was able to proteolytically remove the leader peptide from NisA. Proteolytic removal of the leader peptide by ElxP during the biosynthesis of epilancin 15X exposes an N-terminal dehydroalanine on the core peptide of ElxA that hydrolyzes to a pyruvyl group. The short-chain dehydrogenase ElxO reduces the pyruvyl group to a lactyl moiety in the final step of epilancin 15X maturation. Using synthetic peptides, we also investigated the substrate specificity of ElxO and determined the 1.85 Å resolution X-ray crystal structure of the enzyme.

PubMed: 24866416
DOI: 10.1021/cb5002526

Experimental method

X-RAY DIFFRACTION (1.9 Å)