2.6.1.52: phosphoserine transaminase
This is an abbreviated version!
For detailed information about phosphoserine transaminase, go to the full flat file.
Reaction
Synonyms
3-O-phospho-L-serine:2-oxoglutarate aminotransferase, 3-phosphoserine aminotransferase, AspAT, AtPSAT, AtPSAT1, BCIR PSAT, bmPSAT, EhPSAT, hydroxypyruvic phosphate-glutamic transaminase, L-phosphoserine aminotransferase, phosphohydroxypyruvate transaminase, phosphohydroxypyruvic-glutamic transaminase, phosphoserine aminotransferase, phosphoserine aminotransferase 1, phosphoserine aminotransferase1, phosphoserine aminotransferase2, phosphoserine aminotransferases, PSAT, PSAT alpha, PSAT beta, PSAT-BALC, PSAT-BCIRA, PSAT-ECOLI, PSAT1, PSAT2, PSerAT, serC, sll1559
ECTree
2.6.1.52 phosphoserine transaminaseAdvanced search results
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results (Crystallization
Crystallization on EC 2.6.1.52 - phosphoserine transaminase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
comparison with enzyme structure from Escherichia coli and Bacillus circulans
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in presence or absence of L-phosphoserine, to resolutions of 1.5 and 1.6 A, respectively. Substrate binding induces local conformational changes. No domain or subunit movements are observed. Residues Arg42 and Arg328 and His41 and His327 form a tight binding site for the phosphate group of L-phosphoserine
three crystal structures of isozyme AtPSAT1 are captured at different stages of the reaction: (i) internal aldimine state with PLP covalently bound to the catalytic K265, (ii) holoenzyme in complex with pyridoxamine-50-phosphate (PMP) after transfer of the amino group from glutamate and (iii) the geminal diamine intermediate state wherein the cofactor is covalently bound to both, K265 and PSer. These snapshots over the course of the reaction present the detailed architecture of AtPSAT1. Purified detagged recombinant enzyme in complex with cofactor PLP or pyridoxamine or product phosphoserine, sitting drop method, mixing of 15 mg/ml protein and 1 mM ligand (PLP, PMP) or 50 mM ligand (PSer) in 25 mM HEPES, pH 7.4, 100 mM KCl, 50 mM NaCl, and 1 mM TCEP with crystallization solution containing 0.2 M lithium sulfate, 17% PEG 3350, and 0.1 M Tris at pH 8.5 for ATPSAT1-PLP, with 0.2 M lithium sulfate, 17% PEG 3350, and 0.1 M Tris at pH 8.5, and 10 mM glutamate for AtPSAT1-PMP, and with 19% PEG 3350 and 0.1 M Tris at pH 8.5 for AtPSAT1-PSer, xadX-ray diffraction structure determination and analysis at 1.57-1.70 A resolution
energy-minimized average simulated model. the enzyme exists as a homodimer and each subunit of the protein is composed of two domains, a large pyridoxal phosphate-binding domain and a C-terminal domain. The enzyme harbors two active sites present at the subunit interface. The indole ring of residue Trp101 stacks with the pyridine ring of pyridoxal 5'-phopsphate at the active site and distance between the two moieties is about 5 A
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purified wild-type enzyme and enzyme mutants EhPSAT_DELTA45 and EhPSAT_DELTA4 in complex with cofactor pyridoxal-5'phosphate, hanging drop vapour diffusion method, mixing of protein solution with precipitant solution containing 25-30% PEG 3350 w/v, 100 mM Tris, pH 6.5, 200 mM sodium formate, and 5% glycerol v/v for the wild-type complex, and 25% PEG 2000 MME, and 100 mM potassium thiocyanate for mutant EhPSAT_DELTA45 , and 20% PEG 2000 MME, 100 mM Tris, pH 8.5, and 200 mM TMAO for mutant EhPSAT_DELTA4, all at 16°C and at room temperature, X-ray diffraction structure determination and analysis at 3.0, 1.8, and 2.4 A resolution, respectively, modeling
in complex with cofactor pyridoxal 5'-phosphate, to 1.5 A resolution. The enzyme has a fold typical of the aspartate aminotransferase family of pyridoxal phosphate-dependent enzymes. The protein forms a stable symmetrical homodimer which is maintained by extensive interactions, mostly between the large domains of the two subunits. Each active site contains a bound cofactor molecule. The aromatic ring rests above the C-terminal end of the central strand 7 of the seven-stranded beta-sheet in a pocket in which its pyridine N-atom points in towards the interior of the large domain, hydrogen-bonded to the invariant residue Asp176, and its 5'-phosphate and C4 substituent point out into the dimer interface. The phosphate group is adjacent to the N-terminus of helix 3, hydrogen-bonded to the main-chain amide N-atoms of Ala84 and Thr85 and the side chain of Gln199 from one monomer, as well as to Asn251 and Thr252 of the opposing monomer
hanging-drop vapor diffusion method at 22°C crystal. Structure of phosphoserine aminotransferase is determined at 1.2 and 1.5 A resolution at pH 8.5 and 4.6, respectively
to 2.15 A resolution. The active site is in a closed conformation, and pyridoxal 5'-phosphate forms an internal aldimine linkage to Lys 202. Residue Val 340 near the active site might be responsible in closing the active site
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