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ATOMIC-STRUCTURE AT 2.5 ANGSTROM RESOLUTION OF URIDINE PHOSPHORYLASE FROM ESCHERICHIA-COLI AS REFINED IN THE MONOCLINIC CRYSTAL-LATTICE

被引：52
作者：
MORGUNOVA, EY
MIKHAILOV, AM
POPOV, AN
BLAGOVA, EV
SMIRNOVA, EA
VAINSHTEIN, BK
MAO, C
ARMSTRONG, SR
EALICK, SE
KOMISSAROV, AA
LINKOVA, EV
BURLAKOVA, AA
MIRONOV, AS
DEBABOV, VG
机构：
[1] RUSSIAN ACAD SCI,INST CRYSTALLOG,MOSCOW 117333,RUSSIA
[2] CORNELL UNIV,BIOCHEM MOLEC & CELL BIOL SECT,ITHACA,NY 14853
[3] RUSSIAN GNIIGENETIKA,STATE SCI CTR,MOSCOW 113545,RUSSIA
来源：
FEBS LETTERS | 1995年 / 367卷 / 02期
关键词：
URIDINE PHOSPHORYLASE; ESCHERICHIA-COLI; X-RAY STRUCTURE;
D O I：
10.1016/0014-5793(95)00489-V
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：
Uridine phosphorylase from E, coli (Upase) has been crystallized using vapor diffusion technique in a new monoclinic crystal form, The structure was determined by the molecular replacement method at 2.5 Angstrom resolution, The coordinates of the trigonal crystal form were used as a starting model and the refinement by the program XPLOR led to the R-factor of 18.6%, The amino acid fold of the protein was found to be the same as that in the trigonal crystals, The positions of flexible regions were refined, The conclusion about the involvement in the active site is in good agreement with the results of the biochemical experiments.
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页码：183 / 187
页数：5
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