REFINED CRYSTAL-STRUCTURE OF ACINETOBACTER GLUTAMINASIFICANS GLUTAMINASE ASPARAGINASE

被引:42
作者
LUBKOWSKI, J [1 ]
WLODAWER, A [1 ]
HOUSSET, D [1 ]
WEBER, IT [1 ]
AMMON, HL [1 ]
MURPHY, KC [1 ]
SWAIN, AL [1 ]
机构
[1] UNIV MARYLAND,DEPT CHEM & BIOCHEM,COLLEGE PK,MD 20742
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1994年 / 50卷
关键词
D O I
10.1107/S0907444994003446
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The crystal structure of glutaminase-asparaginase from Acinetobacter glutaminasificans has been reinterpreted and refined to an R factor of 0.171 at 2.9 Angstrom resolution, using the same X-ray diffraction data that were used to build a preliminary model of this enzyme [Ammon, Weber, Wlodawer, Harrison, Gilliland, Murphy, Sjolin and Roberts (1988). J. Biol. Chem. 263, 150-156]. The current model, which does not include solvent, is based in part on the related structure of Escherichia coli asparaginase and is significantly different from the structure of the enzyme from A. glutaminasificans described previously. The reason for the discrepancies has been traced to insufficient phasing power of the original heavy-atom derivative data, which could not be compensated for fully by electron-density modification techniques. The corrected structure of A. glutaminasificans glutaminase-asparaginase is presented and compared with the preliminary model and with the structure of E. coli asparaginase.
引用
收藏
页码:826 / 832
页数:7
相关论文
共 25 条
[1]  
AMMON HL, 1988, J BIOL CHEM, V263, P150
[2]   THE MOLECULAR SYMMETRY OF GLUTAMINASE-ASPARAGINASES - ROTATION FUNCTION STUDIES OF THE PSEUDOMONAS-7A AND ACINETOBACTER ENZYMES [J].
AMMON, HL ;
MURPHY, KC ;
SJOLIN, L ;
WLODAWER, A ;
HOLCENBERG, JS ;
ROBERTS, J .
ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE CRYSTAL ENGINEERING AND MATERIALS, 1983, 39 (APR) :250-257
[3]   ON THE ROLE OF HISTIDINE AND TYROSINE RESIDUES IN ESCHERICHIA-COLI ASPARAGINASE - CHEMICAL MODIFICATION AND H-1-NUCLEAR MAGNETIC-RESONANCE STUDIES [J].
BAGERT, U ;
ROHM, KH .
BIOCHIMICA ET BIOPHYSICA ACTA, 1989, 999 (01) :36-41
[4]   SLOW-COOLING PROTOCOLS FOR CRYSTALLOGRAPHIC REFINEMENT BY SIMULATED ANNEALING [J].
BRUNGER, AT ;
KRUKOWSKI, A ;
ERICKSON, JW .
ACTA CRYSTALLOGRAPHICA SECTION A, 1990, 46 :585-593
[5]   PROBING THE ROLE OF THREONINE AND SERINE RESIDUES OF ESCHERICHIA-COLI ASPARAGINASE-II BY SITE-SPECIFIC MUTAGENESIS [J].
DERST, C ;
HENSELING, J ;
ROHM, KH .
PROTEIN ENGINEERING, 1992, 5 (08) :785-789
[6]   A LEAST-SQUARES REFINEMENT METHOD FOR ISOMORPHOUS REPLACEMENT [J].
DICKERSO.RE ;
WEINZIER.JE ;
PALMER, RA .
ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL CRYSTALLOGRAPHY AND CRYSTAL CHEMISTRY, 1968, B 24 :997-&
[7]   CRYSTALLOGRAPHIC EVIDENCE FOR TETRAMERIC SUBUNIT STRUCTURE OF L-ASPARAGINASE FROM ESCHERICHIA-COLI [J].
EPP, O ;
STEIGEMA.W ;
FORMANEK, H ;
HUBER, R .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1971, 20 (03) :432-&
[8]   INCORPORATION OF FAST FOURIER-TRANSFORMS TO SPEED RESTRAINED LEAST-SQUARES REFINEMENT OF PROTEIN STRUCTURES [J].
FINZEL, BC .
JOURNAL OF APPLIED CRYSTALLOGRAPHY, 1987, 20 :53-55
[9]   HISTOGRAM SPECIFICATION AS A METHOD OF DENSITY MODIFICATION [J].
HARRISON, RW .
JOURNAL OF APPLIED CRYSTALLOGRAPHY, 1988, 21 :949-952
[10]  
HENDRICKSON WA, 1985, METHOD ENZYMOL, V115, P252