Structure of SAICAR synthetase from Pyrococcus horikoshii OT3: Insights into thermal stability

被引:7
|
作者
Manjunath, Kavyashree [1 ]
Kanaujia, Shankar Prasad [2 ]
Kanagaraj, Surekha [3 ]
Jeyakanthan, Jeyaraman [3 ]
Sekar, Kanagaraj [1 ]
机构
[1] Indian Inst Sci, Supercomp Educ & Res Ctr, Bangalore 560012, Karnataka, India
[2] Indian Inst Technol, Dept Biotechnol, Gauhati 781039, India
[3] Alagappa Univ, Dept Bioinformat, Karaikkudi 630003, Tamil Nadu, India
关键词
SAICAR synthetase; Purine de novo biosynthesis; Pyrococcus horikoshii OT3; Hyperthermophile; Thermostable proteins; HYPERTHERMOPHILIC ENZYMES; PROTEIN THERMOSTABILITY; THERMOTOGA-MARITIMA; POTENTIAL FUNCTIONS; SECONDARY STRUCTURE; SYNTHASE; RIBONUCLEOTIDE; BIOSYNTHESIS; CARBOXYLASE; MECHANISM;
D O I
10.1016/j.ijbiomac.2012.10.028
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 first native crystal structure of Phosphoribosylaminoimidazole-succinocarboxamide synthetase (SAICAR synthetase) from a hyperthermophilic organism Pyrococcus horikoshii OT3 was determined in two space groups H3 (Type-1: Resolution 2.35 angstrom) and in C222(1) (Type-2: Resolution 1.9 angstrom). Both are dimeric but Type-1 structure exhibited hexameric arrangement due to the presence of cadmium ions. A comparison has been made on the sequence and structures of all SAICAR synthetases to better understand the differences between mesophilic, thermophilic and hyperthermophilic SAICAR synthetases. These SAICAR synthetases are reasonably similar in sequence and three-dimensional structure; however, differences were visible only in the subtler details of percentage composition of the sequences, salt bridge interactions and non-polar contact areas. (c) 2012 Elsevier B.V. All rights reserved.
引用
收藏
页码:7 / 19
页数:13
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