X-ray diffraction study of the complexes of SAICAR synthase with adenosinetriphosphate

被引:9
作者
Antonyuk, SV
Grebenko, AI
Levdikov, VM
Urusova, DV
Melik-Adamyan, VR
Lamzin, VS
Wilson, KS
机构
[1] Russian Acad Sci, Shubnikov Inst Crystallog, Moscow 117333, Russia
[2] European Mol Biol Lab, Hamburg Outstn, DESY, D-22603 Hamburg, Germany
基金
俄罗斯基础研究基金会;
关键词
D O I
10.1134/1.1387127
中图分类号
O7 [晶体学];
学科分类号
0702 ; 070205 ; 0703 ; 080501 ;
摘要
The three-dimensional structures of two enzyme-substrate complexes of SAICAR synthase from the yeast Saccharomyces cerevisiae with adenosinetriphosphate (ATP) prepared under different conditions were studied by X-ray diffraction analysis and then refined. An enzyme molecule was shown to contain two binding sites of ATR One of these sites is located in the central cavity of the enzyme molecule and apparently binds the ATP molecule directly involved in the enzymatic reaction. In the complexes, the phosphate groups of ATP occupying this site adopt different conformations depending on the Mg2+ concentration. The functional role of the second binding site located at a distance of approximately 15 Angstrom from the first site away from the central enzyme cavity has not been understood as yet. It might be that the second site perform the regulatory role in enzyme functioning. (C) 2001 MAIK "Nauka/Interperiodica".
引用
收藏
页码:620 / 625
页数:6
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