4FL0

Crystal structure of ALD1 from Arabidopsis thaliana

Summary for 4FL0

• Entry DOI: 10.2210/pdb4fl0/pdb
• Descriptor: Aminotransferase ALD1, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• Functional Keywords: structural genomics, protein structure initiative, israel structural proteomics center, ispc, sandwich fold and architecture, pathogen resistance, plp nbinding, transferase
• Biological source: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• Total number of polymer chains: 2
• Total formula weight: 101764.58

Authors

Sobolev, V.,Edelman, M.,Dym, O.,Unger, T.,Albeck, S.,Kirma, M.,Galili, G.,Israel Structural Proteomics Center (ISPC) (deposition date: 2012-06-14, release date: 2013-02-20, Last modification date: 2024-02-28)

Primary citation

Sobolev, V.,Edelman, M.,Dym, O.,Unger, T.,Albeck, S.,Kirma, M.,Galili, G.
Structure of ALD1, a plant-specific homologue of the universal diaminopimelate aminotransferase enzyme of lysine biosynthesis.
Acta Crystallogr.,Sect.F, 69:84-89, 2013

PubMed Abstract: Diaminopimelate aminotransferase (DAP-AT) is an enzyme in the lysine-biosynthesis pathway. Conversely, ALD1, a close homologue of DAP-AT in plants, uses lysine as a substrate in vitro. Both proteins require pyridoxal-5'-phosphate (PLP) for their activity. The structure of ALD1 from the flowering plant Arabidopsis thaliana (AtALD1) was solved at a resolution of 2.3 Å. Comparison of AtALD1 with the previously solved structure of A. thaliana DAP-AT (AtDAP-AT) revealed similar interactions with PLP despite sequence differences within the PLP-binding site. However, sequence differences between the binding site of AtDAP-AT for malate, a purported mimic of substrate binding, and the corresponding site in AtALD1 led to different interactions. This suggests that either the substrate itself, or the substrate-binding mode, differs in the two proteins, supporting the known in vitro findings.

PubMed: 23385743
DOI: 10.1107/S1744309112050270

Experimental method

X-RAY DIFFRACTION (2.3 Å)