Acetobacter turbidans α-amino acid ester hydrolase:: merohedral twinning in P21 obscured by pseudo-translational NCS

被引:20
作者
Barends, TRM [1 ]
Dijkstra, BW [1 ]
机构
[1] Univ Groningen, NL-9747 AG Groningen, Netherlands
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2003年 / 59卷
关键词
D O I
10.1107/S0907444903020729
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The structure elucidation of the alpha-amino acid ester hydrolase from Acetobacter turbidans by molecular replacement is described. In the monoclinic crystal, the molecules are related by both rotational and pseudo-crystallographic translational NCS (non-crystallographic symmetry). Refinement of the structure converged at unacceptably high R factors. After re-evaluation of the data, it was found that the crystal was merohedrally twinned, with a high twinning fraction. It is shown that the pseudo-crystallographic NCS causes aberrant behaviour of conventional twinning indicators, which explains why the twinning was only realized at the refinement stage.
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收藏
页码:2237 / 2241
页数:5
相关论文
共 26 条
[1]   THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].
BAILEY, S .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 :760-763
[2]   The sequence and crystal structure of the α-amino acid ester hydrolase from Xanthomonas citri define a new family of β-lactam antibiotic acylases [J].
Barends, TRM ;
Polderman-Tijmes, JJ ;
Jekel, PA ;
Hensgens, CMH ;
de Vries, EJ ;
Janssen, DB ;
Dijkstra, BW .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (25) :23076-23084
[3]   X-ray analysis of two antibiotic-synthesizing bacterial ester hydrolases: preliminary results [J].
Barends, TRM ;
Hensgens, CMH ;
Polderman-Tijmes, JJ ;
Jekel, PA ;
de Vries, E ;
Janssen, DB ;
Dijkstra, BW .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2003, 59 :158-160
[4]  
BARENDS TRM, 2003, UNPUB
[6]   Crystallographic refinement by simulated annealing: Methods and applications [J].
Brunger, AT ;
Rice, LM .
MACROMOLECULAR CRYSTALLOGRAPHY, PT B, 1997, 277 :243-269
[7]   Crystallography & NMR system:: A new software suite for macromolecular structure determination [J].
Brunger, AT ;
Adams, PD ;
Clore, GM ;
DeLano, WL ;
Gros, P ;
Grosse-Kunstleve, RW ;
Jiang, JS ;
Kuszewski, J ;
Nilges, M ;
Pannu, NS ;
Read, RJ ;
Rice, LM ;
Simonson, T ;
Warren, GL .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1998, 54 :905-921
[8]   A twinned monoclinic crystal form of human peroxiredoxin 5 with eight molecules in the asymmetric unit [J].
Declercq, JP ;
Evrard, C .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2001, 57 :1829-1835
[9]   Stabilization of a tetrameric enzyme (α-amino acid ester hydrolase from Acetobacter turbidans) enables a very improved performance of ampicillin synthesis [J].
Fernandez-Lafuente, R ;
Hernández-Jústiz, O ;
Mateo, C ;
Terreni, M ;
Alonso, J ;
Garcia-López, JL ;
Moreno, MA ;
Guisan, JM .
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2001, 11 (4-6) :633-638
[10]   STRUCTURE OF DEOXYHEMOGLOBIN OF THE ANTARCTIC FISH PAGOTHENIA-BERNACCHII WITH AN ANALYSIS OF THE STRUCTURAL BASIS OF THE ROOT EFFECT BY COMPARISON OF THE LIGANDED AND UNLIGANDED HEMOGLOBIN STRUCTURES [J].
ITO, N ;
KOMIYAMA, NH ;
FERMI, G .
JOURNAL OF MOLECULAR BIOLOGY, 1995, 250 (05) :648-658