4AZK

Structural basis of L-phosphoserine binding to Bacillus alcalophilus phosphoserine aminotransferase

Summary for 4AZK

• Entry DOI: 10.2210/pdb4azk/pdb
• Related: 1W23 2BHX 2BI1 2BI2 2BI3 2BI5 2BI9 2BIA 2BIE 2BIG 4AZJ
• Descriptor: PHOSPHOSERINE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: transferase, pyridoxal phosphate
• Biological source: BACILLUS ALCALOPHILUS
• Total number of polymer chains: 2
• Total formula weight: 81052.31

Authors

Battula, P.,Dubnovitsky, A.P.,Papageorgiou, A.C. (deposition date: 2012-06-26, release date: 2013-05-01, Last modification date: 2023-12-20)

Primary citation

Battula, P.,Dubnovitsky, A.P.,Papageorgiou, A.C.
Structural Basis of L-Phosphoserine Binding to Bacillus Alcalophilus Phosphoserine Aminotransferase
Acta Crystallogr.,Sect.D, 69:804-, 2013

PubMed Abstract: Phosphoserine aminotransferase is a vitamin B6-dependent enzyme that catalyzes the reversible conversion of 3-phosphohydroxypyruvate to L-phosphoserine using glutamate as an amine donor. In an effort to gain insight into the substrate-recognition mechanism of the enzyme, crystal structures of Bacillus alcalophilus phosphoserine aminotransferase in the presence or absence of L-phosphoserine were determined to resolutions of 1.5 and 1.6 Å, respectively. Local conformational changes induced upon substrate binding were identified. However, in contrast to other aminotransferases, no domain or subunit movements were observed. Two Arg residues (Arg42 and Arg328) and two His residues (His41 and His327) were found to form a tight binding site for the phosphate group of L-phosphoserine. Comparison with Escherichia coli phosphoserine aminotransferase in complex with the substrate analogue α-methylglutamate revealed more extensive structural changes in the case of L-phosphoserine binding. Based on the structural analysis, the flexibility of Arg328 is proposed to be critical for substrate recognition.

PubMed: 23633589
DOI: 10.1107/S0907444913002096

Experimental method

X-RAY DIFFRACTION (1.595 Å)