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

页码：3090 / 3096

页数：7

共 50 条

[31] Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity
Takahide Kouno
Tania V. Silvas
Brendan J. Hilbert
Shivender M. D. Shandilya
Markus F. Bohn
Brian A. Kelch
William E. Royer
Mohan Somasundaran
Nese Kurt Yilmaz
Hiroshi Matsuo
Celia A. Schiffer
Nature Communications, 8
[32] Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity
Kouno, Takahide
Silvas, Tania V.
Hilbert, Brendan J.
Shandilya, Shivender M. D.
Bohn, Markus F.
Kelch, Brian A.
Royer, William E.
Somasundaran, Mohan
Yilmaz, Nese Kurt
Matsuo, Hiroshi
Schiffer, Celia A.
NATURE COMMUNICATIONS, 2017, 8
[33] Structural basis for the catalysis and substrate specificity of homoserine kinase
Krishna, SS
Zhou, T
Daugherty, M
Osterman, A
Zhang, H
BIOCHEMISTRY, 2001, 40 (36) : 10810 - 10818
[34] STRUCTURAL BASIS OF SUBSTRATE-SPECIFICITY IN THE SERINE PROTEASES
PERONA, JJ
CRAIK, CS
PROTEIN SCIENCE, 1995, 4 (03) : 337 - 360
[35] Structural basis of substrate specificity in porcine RNase 4
Liang, Shutian
Acharya, K. Ravi
FEBS JOURNAL, 2016, 283 (05) : 912 - 928
[36] The structural basis for catalysis and substrate specificity of a rhomboid protease
Vinothkumar, Kutti R.
Strisovsky, Kvido
Andreeva, Antonina
Christova, Yonka
Verhelst, Steven
Freeman, Matthew
EMBO JOURNAL, 2010, 29 (22): : 3797 - 3809
[37] Structural basis of the substrate specificity of human and bacterial kynureninase
Phillips, R. S.
FEBS JOURNAL, 2013, 280 : 171 - 172
[38] STRUCTURAL BASIS FOR THE SUBSTRATE SPECIFICITY OF PROTEIN TYROSINE PHOSPHATASES
Yang, J.
Cheng, Z.
Niu, T.
Liang, X.
Zhou, G. W.
Zhao, Z. J.
ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, 1999, 55 : 361 - 361
[39] Structural basis for substrate specificity of the human mitochondrial deoxyribonucleotidase
Walldén, K
Ruzzenente, B
Rinaldo-Matthis, A
Bianchi, V
Nordlund, P
STRUCTURE, 2005, 13 (07) : 1081 - 1088
[40] Structural basis of substrate specificity in malate dehydrogenases:: Crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, α-ketomalonate and tetrahydoNAD
Chapman, ADM
Cortés, A
Dafforn, TR
Clarke, AR
Brady, RL
JOURNAL OF MOLECULAR BIOLOGY, 1999, 285 (02) : 703 - 712

← 1 2 3 4 5 →