EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Oligomeric interactions maintain active-site structure in a noncooperative enzyme family.
ジャーナル・号・ページ	EMBO J, Vol. 41, Issue 17, Page e108368, Year 2022
掲載日	2022年9月1日
著者	Yaohui Li / Rongzhen Zhang / Chi Wang / Farhad Forouhar / Oliver B Clarke / Sergey Vorobiev / Shikha Singh / Gaetano T Montelione / Thomas Szyperski / Yan Xu / John F Hunt /
PubMed 要旨	The evolutionary benefit accounting for widespread conservation of oligomeric structures in proteins lacking evidence of intersubunit cooperativity remains unclear. Here, crystal and cryo-EM ...The evolutionary benefit accounting for widespread conservation of oligomeric structures in proteins lacking evidence of intersubunit cooperativity remains unclear. Here, crystal and cryo-EM structures, and enzymological data, demonstrate that a conserved tetramer interface maintains the active-site structure in one such class of proteins, the short-chain dehydrogenase/reductase (SDR) superfamily. Phylogenetic comparisons support a significantly longer polypeptide being required to maintain an equivalent active-site structure in the context of a single subunit. Oligomerization therefore enhances evolutionary fitness by reducing the metabolic cost of enzyme biosynthesis. The large surface area of the structure-stabilizing oligomeric interface yields a synergistic gain in fitness by increasing tolerance to activity-enhancing yet destabilizing mutations. We demonstrate that two paralogous SDR superfamily enzymes with different specificities can form mixed heterotetramers that combine their individual enzymological properties. This suggests that oligomerization can also diversify the functions generated by a given metabolic investment, enhancing the fitness advantage provided by this architectural strategy.
リンク	EMBO J / PubMed:35801308 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	1.59 - 4.28 Å
構造データ	32211 7vyq EMDB-32211, PDB-7vyq: Short chain dehydrogenase (SCR) cryoEM structure with NADP and ethyl 4-chloroacetoacetate 手法: EM (単粒子) / 解像度: 3.13 Å EMDB-32212: Oligomeric interactions maintain active-site structure in a non-cooperative enzyme family 手法: EM (単粒子) / 解像度: 4.03 Å EMDB-32213: Oligomeric interactions maintain active-site structure in a non-cooperative enzyme family 手法: EM (単粒子) / 解像度: 4.28 Å PDB-7dld: Crystal structures of (S)-carbonyl reductases from Candida parapsilosis in different oligomerization states 手法: X-RAY DIFFRACTION / 解像度: 1.75 Å PDB-7dll: Short chain dehydrogenase 2 (SCR2) crystal structure with NADPH 手法: X-RAY DIFFRACTION / 解像度: 1.89 Å PDB-7dlm: Short chain dehydrogenase (SCR) crystal structure with NADPH 手法: X-RAY DIFFRACTION / 解像度: 1.59 Å PDB-7dmg: Short chain dehydrogenase 2 (SCR2) crystal structure with NADP 手法: X-RAY DIFFRACTION / 解像度: 1.79 Å PDB-7dn1: Hetero-oligomers of SCR-SCR2 crystal structure with NADPH 手法: X-RAY DIFFRACTION / 解像度: 1.74 Å
化合物	ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-HOH: WATER ChemComp-NDP: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / NADPH ChemComp-NAP: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE ChemComp-83I: ethyl 4-chloranyl-3-oxidanylidene-butanoate / 4-クロロアセト酢酸エチル
由来	candida parapsilosis (酵母) Candida parapsilosis
キーワード	OXIDOREDUCTASE / Rossman fold / tetramer / tag-free / wild type / wild type with NADPH