Yeast nicotinate-nucleotide pyrophosphorylase in complex with ligand: crystallization and preliminary structural approaches

• 영문명: Yeast nicotinate-nucleotide pyrophosphorylase in complex with ligand: crystallization and preliminary structural approaches
• 발행기관: 한국구조생물학회
• 저자명: Tae Gyun Kim Taek Hun Kwon Hyojeong Choi Min-Kyung Park JoongBae Park In Gyeong Chae Hyun-Jung An
• 간행물 정보: 『Biodesign』Vol 10, No 4, Dec, 73~78쪽, 전체 6쪽
• 주제분류: 자연과학 > 생물학
• 파일형태: PDF
• 발행일자: 2022.12.31

영문 초록

Pyridine-2,3-dicarboxylic acid which is a biologically potent molecule implicated in the neurodegenerative environment is catalyzed by nicotinate-nucleotide pyrophosphorylase (NMnPP) to produce a precursor molecule, nicotinate mononucleotide (NMn), of de novo biosynthesis of the coenzyme nicotinamide adenine dinucleotide (NAD+). The protein preparation, crystallization, and preliminary structural features of full-length enzyme in complex with product reactant suggest that yeast NMnPP acts as stable hexamer formation. Crystals of S. cerevisiae NMnPP were obtained and diffracted to a resolution of 1.74 Å and 1.99 Å for apo and complex forms, belonged to the trigonal symmetry group R32 in the unit-cell parameters of a = b = 155.313, c = 67.507 and a = b = 155.091, c = 69.204, respectively. Based on our comparison of eukaryotic NMnPP structures in the apo and complex forms, we propose functional and structural investigation for product binding and hexamer stabilization.

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INTRODUCTION

RESULTS AND DISCUSSION

METHODS

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