The crystal structure of seabream antiquitin reveals the structural basis of its substrate specificity

被引：17
|
作者：
Tang, Wai-Kwan [1 ]
Wong, Kam-Bo [1 ,2 ]
Lam, Yuk-Man [1 ]
Cha, Sun-Shin [3 ]
Cheng, Christopher H. K. [1 ,2 ]
Fong, Wing-Ping [1 ]
机构：
[1] Chinese Univ Hong Kong, Dept Biochem, Hong Kong, Hong Kong, Peoples R China
[2] Chinese Univ Hong Kong, Ctr Prot Sci & Crystallog, Hong Kong, Hong Kong, Peoples R China
[3] Korea Ocean Res & Dev Inst, Marine Biotechnol & New Mat Res Div, Ansan, South Korea
来源：
FEBS LETTERS | 2008年 / 582卷 / 20期
关键词：
antiquitin; ALDH7; alpha-aminoadipic semialdehyde; x-ray crystallography; site-directed mutagenesis; pyridoxine-dependent epilepsy;
D O I：
10.1016/j.febslet.2008.07.059
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The crystal structure of seabream antiquitin in complex with the cofactor NAD(+) was solved at 2.8 angstrom resolution. The mouth of the substrate-binding pocket is guarded by two conserved residues, Glu120 and Arg300. To test the role of these two residues, we have prepared the two mutants E120A and R300A. Our model and kinetics data suggest that antiquitin's specificity towards the substrate alpha-aminoadipic semialdehyde is contributed mainly by Glu120 which interacts with the alpha-amino group of the substrate. On the other hand, Arg300 does not have any specificity interaction with the alpha-carboxylate group of the substrate, but is important in maintaining the active site conformation. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码：3090 / 3096
页数：7
相关论文
共 50 条
  • [41] Crystal structures of human NUDT5 reveal insights into the structural basis of the substrate specificity
    Zha, Manwu
    Zhong, Chen
    Peng, Yingjie
    Hu, Hongyu
    Ding, Jianping
    JOURNAL OF MOLECULAR BIOLOGY, 2006, 364 (05) : 1021 - 1033
  • [42] The structural basis for substrate specificity in DNA topoisomerase IV
    Corbett, KD
    Schoeffler, AJ
    Thomsen, ND
    Berger, JM
    JOURNAL OF MOLECULAR BIOLOGY, 2005, 351 (03) : 545 - 561
  • [43] Structural basis for elastolytic substrate specificity in rodent α-chymases
    Kervinen, Jukka
    Abad, Marta
    Crysler, Carl
    Kolpak, Michael
    Mahan, Andrew D.
    Masucci, John A.
    Bayoumy, Shariff
    Cummings, Maxwell D.
    Yao, Xiang
    Olson, Matthew
    de Garavilla, Lawrence
    Kuo, Lawrence
    Deckman, Ingrid
    Spurlino, John
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (01) : 427 - 436
  • [44] Author Correction: Laminarinase from Flavobacterium sp. reveals the structural basis of thermostability and substrate specificity
    Hui-Min Qin
    Takuya Miyakawa
    Akira Inoue
    Akira Nakamura
    Ryuji Nishiyama
    Takao Ojima
    Masaru Tanokura
    Scientific Reports, 8
  • [45] Crystal structure analysis of Bacillus subtilis ferredoxin-NADP+ oxidoreductase and the structural basis for its substrate selectivity
    Komori, Hirofumi
    Seo, Daisuke
    Sakurai, Takeshi
    Higuchi, Yoshiki
    PROTEIN SCIENCE, 2010, 19 (12) : 2279 - 2290
  • [46] Crystal structure of isoamyl acetate-hydrolyzing esterase from Saccharomyces cerevisiae reveals a novel active site architecture and the basis of substrate specificity
    Ma, Jinming
    Lu, Qianda
    Yuan, Ye
    Ge, Honghua
    Li, Kuai
    Zhao, Wei
    Gao, Yongxiang
    Niu, Liwen
    Teng, Maikun
    PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2011, 79 (02) : 662 - 668
  • [47] Crystal structure of human phosphodiesterase 3B: Atomic basis for substrate and inhibitor specificity
    Scapin, G
    Patel, SB
    Chung, C
    Varnerin, JP
    Edmondson, SD
    Mastracchio, A
    Parmee, ER
    Singh, SB
    Becker, JW
    Van der Ploeg, LHT
    Tota, MR
    BIOCHEMISTRY, 2004, 43 (20) : 6091 - 6100
  • [48] Determination of the crystal structure and substrate specificity of ananain
    Tang Yongqing
    Wilmann, Pascal G.
    Pan, Jing
    West, Michael L.
    Brown, Tracey J.
    Mynott, Tracey
    Pike, Robert N.
    Wijeyewickrema, Lakshmi C.
    BIOCHIMIE, 2019, 166 : 194 - 202
  • [49] The crystal structure of human forkhead box N1 in complex with DNA reveals the structural basis for forkhead box family specificity
    Newman, Joseph A.
    Aitkenhead, Hazel
    Gavard, Angeline E.
    Rota, Ioanna A.
    Handel, Adam E.
    Hollander, Georg A.
    Gileadi, Opher
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2020, 295 (10) : 2948 - 2958
  • [50] Structural features of the Nostoc punctiforme debranching enzyme reveal the basis of its mechanism and substrate specificity
    Dumbrepatil, Arti Baban
    Choi, Ji-Hye
    Park, Jong Tae
    Kim, Myo-Jeong
    Kim, Tae Jip
    Woo, Eui-Jeon
    Park, Kwan Hwa
    PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2010, 78 (02) : 348 - 356
12345