3BS8

Crystal structure of Glutamate 1-Semialdehyde Aminotransferase complexed with pyridoxamine-5'-phosphate From Bacillus subtilis

3BS8 の概要

• エントリーDOI: 10.2210/pdb3bs8/pdb
• 分子名称: Glutamate-1-semialdehyde 2,1-aminomutase, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• 機能のキーワード: glutamate-1-semialdehyde 2, 1-aminotransferase, porphyrin biosynthesis, isomerase, pyridoxal phosphate
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm (Potential): P30949
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47772.98

構造登録者

Ge, H.,Fan, J.,Teng, M.,Niu, L. (登録日: 2007-12-22, 公開日: 2008-12-23, 最終更新日: 2023-11-01)

主引用文献

Ge, H.,Lv, X.,Fan, J.,Gao, Y.,Teng, M.,Niu, L.
Crystal structure of Glutamate1-semialdehyde aminotransferase from Bacillus subtilis with bound pyridoxamine-5'-phosphate
Biochem.Biophys.Res.Commun., 402:356-360, 2010

PubMed Abstract: Glutamate-1-semialdehyde aminotransferase (GSA-AT), also named glutamate-1-semialdehyde aminomutase (GSAM), a pyridoxamine-5'-phosphate (PMP)/pyridoxal-5'-phosphate (PLP) dependent enzyme, catalyses the transamination of the substrate glutamate-1-semialdehyde (GSA) to the product 5-Aminolevulinic acid (ALA) by an unusual intramolecular exchange of amino and oxo groups within the catalytic intermediate 4,5-diaminovalerate (DAVA). This paper presents the crystal structure of GSA-AT from Bacillus subtilis (GSA-ATBsu) in its PMP-bound form at 2.3Å resolution. The structure was determined by molecular replacement using the Synechococcus GSAM (GSAMSyn) structure as a search model. Unlike the previous reported GSAM/GSA-AT structures, GSA-ATBsu is a symmetric homodimer in the PMP-bound form, which shows the structural symmetry at the gating loop region with open state, as well as identical cofactor (PMP) binding in each monomer. This observation of PMP in combination with an "open" lid supports one characteristic feature for this enzyme, as the catalyzed reaction is believed to be initiated by PMP. Furthermore, the symmetry of GSA-ATBsu structure challenges the previously proposed negative cooperativity between monomers of this enzyme.

PubMed: 20946885
DOI: 10.1016/j.bbrc.2010.10.033

実験手法

X-RAY DIFFRACTION (2.3 Å)