Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Oligomeric interactions maintain active-site structure in a noncooperative enzyme family.
Journal, issue, pages	EMBO J, Vol. 41, Issue 17, Page e108368, Year 2022
Publish date	Sep 1, 2022
Authors	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 Abstract	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.
External links	EMBO J / PubMed:35801308 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.59 - 4.28 Å
Structure data	32211 7vyq EMDB-32211, PDB-7vyq: Short chain dehydrogenase (SCR) cryoEM structure with NADP and ethyl 4-chloroacetoacetate Method: EM (single particle) / Resolution: 3.13 Å EMDB-32212: Oligomeric interactions maintain active-site structure in a non-cooperative enzyme family Method: EM (single particle) / Resolution: 4.03 Å EMDB-32213: Oligomeric interactions maintain active-site structure in a non-cooperative enzyme family Method: EM (single particle) / Resolution: 4.28 Å PDB-7dld: Crystal structures of (S)-carbonyl reductases from Candida parapsilosis in different oligomerization states Method: X-RAY DIFFRACTION / Resolution: 1.75 Å PDB-7dll: Short chain dehydrogenase 2 (SCR2) crystal structure with NADPH Method: X-RAY DIFFRACTION / Resolution: 1.89 Å PDB-7dlm: Short chain dehydrogenase (SCR) crystal structure with NADPH Method: X-RAY DIFFRACTION / Resolution: 1.59 Å PDB-7dmg: Short chain dehydrogenase 2 (SCR2) crystal structure with NADP Method: X-RAY DIFFRACTION / Resolution: 1.79 Å PDB-7dn1: Hetero-oligomers of SCR-SCR2 crystal structure with NADPH Method: X-RAY DIFFRACTION / Resolution: 1.74 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-HOH: WATER ChemComp-NDP: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE ChemComp-NAP: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE ChemComp-83I: ethyl 4-chloranyl-3-oxidanylidene-butanoate
Source	candida parapsilosis (yeast) Candida parapsilosis
Keywords	OXIDOREDUCTASE / Rossman fold / tetramer / tag-free / wild type / wild type with NADPH