Crystallization and preliminary X-ray analysis of porcine muscle prolyl oligopeptidase

被引:6
作者
Bocskei, Z
Fuxreiter, M
Naray-Szabo, G
Szabo, E
Polgar, L
机构
[1] Chinoin Chem & Pharmaceut Works Ltd, Dept Chem Res, H-1325 Budapest, Hungary
[2] Eotvos Lorand Univ, Dept Theoret Chem, H-1518 Budapest, Hungary
[3] Agr Biotechnol Ctr, Inst Biochem & Prot Res, H-2101 Godollo, Hungary
[4] Hungarian Acad Sci, Biol Res Ctr, Inst Enzymol, H-1518 Budapest, Hungary
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 1998年 / 54卷
关键词
D O I
10.1107/S0907444998004181
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Prolyl oligopeptidase from pig muscle has been crystallized in complex with an inhibitor, using PEG 8000 and calcium acetate as precipitants. The crystals are orthorombic and the space group is P2(1)2(1)2(1) With cell dimensions a = 111.8, b = 101.8, c = 72.4 Angstrom. The asymmetric unit contains a single chain of prolyl oligopeptidase,corresponding to a specific volume of 2.55 Angstrom(3) Da(-1) and solvent-content of 52%. The observed diffraction pattern extends to 2.3 Angstrom resolution and the native crystals are well suited for structural analysis by X-ray diffraction methods.
引用
收藏
页码:1414 / 1415
页数:2
相关论文
共 15 条
[1]   OLIGOPEPTIDASES, AND THE EMERGENCE OF THE PROLYL OLIGOPEPTIDASE FAMILY [J].
BARRETT, AJ ;
RAWLINGS, ND .
BIOLOGICAL CHEMISTRY HOPPE-SEYLER, 1992, 373 (07) :353-360
[2]   A SERINE PROTEASE TRIAD FORMS THE CATALYTIC CENTER OF A TRIACYLGLYCEROL LIPASE [J].
BRADY, L ;
BRZOZOWSKI, AM ;
DEREWENDA, ZS ;
DODSON, E ;
DODSON, G ;
TOLLEY, S ;
TURKENBURG, JP ;
CHRISTIANSEN, L ;
HUGEJENSEN, B ;
NORSKOV, L ;
THIM, L ;
MENGE, U .
NATURE, 1990, 343 (6260) :767-770
[3]   THE PURIFICATION, CHARACTERIZATION AND ANALYSIS OF PRIMARY AND SECONDARY-STRUCTURE OF PROLYL OLIGOPEPTIDASE FROM HUMAN-LYMPHOCYTES - EVIDENCE THAT THE ENZYME BELONGS TO THE ALPHA/BETA HYDROLASE FOLD FAMILY [J].
GOOSSENS, F ;
DEMEESTER, I ;
VANHOOF, G ;
HENDRIKS, D ;
VRIEND, G ;
SCHARPE, S .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1995, 233 (02) :432-441
[4]   Low barrier hydrogen bond is absent in the catalytic triads in the ground state but is present in a transition-state complex in the prolyl oligopeptidase family of serine proteases [J].
Kahyaoglu, A ;
Haghjoo, K ;
Guo, FS ;
Jordan, F ;
Kettner, C ;
Felfoldi, F ;
Polgar, L .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (41) :25547-25554
[5]   SOLVENT CONTENT OF PROTEIN CRYSTALS [J].
MATTHEWS, BW .
JOURNAL OF MOLECULAR BIOLOGY, 1968, 33 (02) :491-+
[6]   STRUCTURAL RELATIONSHIP BETWEEN LIPASES AND PEPTIDASES OF THE PROLYL OLIGOPEPTIDASE FAMILY [J].
POLGAR, L .
FEBS LETTERS, 1992, 311 (03) :281-284
[7]  
POLGAR L, 1994, METHOD ENZYMOL, V244, P188
[8]   PROLYL ENDOPEPTIDASE AND DIPEPTIDYL PEPTIDASE-IV ARE DISTANTLY RELATED MEMBERS OF THE SAME FAMILY OF SERINE PROTEASES [J].
POLGAR, L ;
SZABO, E .
BIOLOGICAL CHEMISTRY HOPPE-SEYLER, 1992, 373 (07) :361-366
[9]   A NEW FAMILY OF SERINE-TYPE PEPTIDASES RELATED TO PROLYL OLIGOPEPTIDASE [J].
RAWLINGS, ND ;
POLGAR, L ;
BARRETT, AJ .
BIOCHEMICAL JOURNAL, 1991, 279 :907-908
[10]   CDNA CLONING OF PORCINE BRAIN PROLYL ENDOPEPTIDASE AND IDENTIFICATION OF THE ACTIVE-SITE SERYL RESIDUE [J].
RENNEX, D ;
HEMMINGS, BA ;
HOFSTEENGE, J ;
STONE, SR .
BIOCHEMISTRY, 1991, 30 (08) :2195-2203