4LMB

Crystal structure analysis of O-acetylserine sulfhydrylase CysK2 complexed with cystine from Microcystis aeruginosa 7806

4LMB の概要

• エントリーDOI: 10.2210/pdb4lmb/pdb
• 関連するPDBエントリー: 4LMA
• 分子名称: Cysteine synthase, CYSTEINE, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: sulfhydrylase, transferase
• 由来する生物種: Microcystis aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35234.25

構造登録者

Lu, M. (登録日: 2013-07-10, 公開日: 2014-06-04, 最終更新日: 2023-11-15)

主引用文献

Lu, M.,Xu, B.Y.,Zhou, K.,Cheng, W.,Jiang, Y.L.,Chen, Y.,Zhou, C.Z.
Structural and biochemical analyses of Microcystis aeruginosa O-acetylserine sulfhydrylases reveal a negative feedback regulation of cysteine biosynthesis.
Biochim.Biophys.Acta, 1844:308-315, 2014

PubMed Abstract: O-acetylserine sulfhydrylase (OASS) catalyzes the final step of cysteine biosynthesis from O-acetylserine (OAS) and inorganic sulfide in plants and bacteria. Bioinformatics analyses combined with activity assays enabled us to annotate the two putative genes of Microcystis aeruginosa PCC 7806 to CysK1 and CysK2, which encode the two 75% sequence-identical OASS paralogs. Moreover, we solved the crystal structures of CysK1 at 2.30Ǻ and cystine-complexed CysK2 at 1.91Ǻ, revealing a quite similar overall structure that belongs to the family of fold-type II PLP-dependent enzymes. Structural comparison indicated a significant induced fit upon binding to the cystine, which occupies the binding site for the substrate OAS and blocks the product release tunnel. Subsequent enzymatic assays further confirmed that cystine is a competitive inhibitor of the substrate OAS. Moreover, multiple-sequence alignment revealed that the cystine-binding residues are highly conserved in all OASS proteins, suggesting that this auto-inhibition of cystine might be a universal mechanism of cysteine biosynthesis pathway.

PubMed: 24275508
DOI: 10.1016/j.bbapap.2013.11.008

実験手法

X-RAY DIFFRACTION (1.91 Å)