5G4J

Phospholyase A1RDF1 from Arthrobacter in complex with phosphoethanolamine

Summary for 5G4J

• Entry DOI: 10.2210/pdb5g4j/pdb
• Related: 5G4I
• Descriptor: PUTATIVE AMINOTRANSFERASE CLASS III PROTEIN, {5-hydroxy-6-methyl-4-[(E)-{[2-(phosphonooxy)ethyl]imino}methyl]pyridin-3-yl}methyl dihydrogen phosphate, SODIUM ION, ... (4 entities in total)
• Functional Keywords: lyase, pyridoxal phosphate, transaminase, phospholyase
• Biological source: ARTHROBACTER AURESCENS
• Total number of polymer chains: 2
• Total formula weight: 96992.08

Authors

Cuetos, A.,Tuan, A.N.,Mangas Sanchez, J.,Grogan, G. (deposition date: 2016-05-13, release date: 2016-10-19, Last modification date: 2024-01-10)

Primary citation

Cuetos, A.,Steffen-Munsberg, F.,Mangas Sanchez, J.,Frese, A.,Bornscheuer, U.T.,Hohne, M.,Grogan, G.
Structural Basis for Phospholyase Activity of a Class III Transaminase Homologue.
Chembiochem, 17:2308-2311, 2016

PubMed Abstract: Pyridoxal-phosphate (PLP)-dependent enzymes catalyse a remarkable diversity of chemical reactions in nature. A1RDF1 from Arthrobacter aurescens TC1 is a fold type I, PLP-dependent enzyme in the class III transaminase (TA) subgroup. Despite sharing 28 % sequence identity with its closest structural homologues, including β-alanine:pyruvate and γ-aminobutyrate:α-ketoglutarate TAs, A1RDF1 displayed no TA activity. Activity screening revealed that the enzyme possesses phospholyase (E.C. 4.2.3.2) activity towards O-phosphoethanolamine (PEtN), an activity described previously for vertebrate enzymes such as human AGXT2L1, enzymes for which no structure has yet been reported. In order to shed light on the distinctive features of PLP-dependent phospholyases, structures of A1RDF1 in complex with PLP (internal aldimine) and PLP⋅PEtN (external aldimine) were determined, revealing the basis of substrate binding and the structural factors that distinguish the enzyme from class III homologues that display TA activity.

PubMed: 27709756
DOI: 10.1002/cbic.201600482

Experimental method

X-RAY DIFFRACTION (1.87 Å)