Crystallization and preliminary X-ray diffraction studies of the peptide methionine sulfoxide reductase B domain of Neisseria meningitidis PILB

被引:13
作者
Kauffmann, B
Favier, D
Olry, A
Boschi-Muller, S
Carpentier, P
Branlant, G
Aubry, A
机构
[1] Lab Cristallog & MOdelisat Mat Mineraux & Biol, Grp Bioscristallog, UMR 7036, F-54506 Vandoeuvre Les Nancy, France
[2] Lab Maturat ARN & Enzymol Mol, UMR 7567, F-54506 Vandoeuvre Les Nancy, France
[3] CEA, CNRS, Inst Biol Struct, Cristallog & Cristallogenese Prot Lab, F-38027 Grenoble, France
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2002年 / 58卷
关键词
D O I
10.1107/S0907444902010570
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Peptide methionine sulfoxide reductases (Msr) are ubiquitous enzymes that catalyse the reduction of free and protein-bound methionine sulfoxide back to methionine via sulfenic acid chemistry. Two classes of Msrs, MsrA and MsrB, have been described. The fact that the two Msrs display opposite stereoselectivities and have no sequence identity suggests that there is no structural similarity between the two classes. No three-dimensional structure of a MsrB is known. In the present report, the MsrB subdomain of Neisseria meningitidis PILB was used to grow orthorhombic crystals by the hanging-drop vapour-diffusion technique. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 44.0, b = 118.6, c = 138.5 Angstrom. Crystals of selenomethionine-substituted MsrB were grown under the same conditions in order to use the MAD method for structure determination. Three diffraction data sets at 1.8 Angstrom resolution were collected. The positions of the Se atoms were determined and should result in a full structure determination.
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页码:1467 / 1469
页数:3
相关论文
共 21 条
[1]   Methods used in the structure determination of bovine mitochondrial F-1 ATPase [J].
Abrahams, JP ;
Leslie, AGW .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1996, 52 :30-42
[2]  
[Anonymous], [No title captured]
[3]   A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli [J].
Boschi-Muller, S ;
Azza, S ;
Sanglier-Cianferani, S ;
Talfournier, F ;
Van Dorsselear, A ;
Branlant, G .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (46) :35908-35913
[4]   CHOOCH:: a program for deriving anomalous-scattering factors from X-ray fluorescence spectra [J].
Evans, G ;
Pettifer, RF .
JOURNAL OF APPLIED CRYSTALLOGRAPHY, 2001, 34 :82-86
[5]   Repair of oxidized proteins - Identification of a new methionine sulfoxide reductase [J].
Grimaud, R ;
Ezraty, B ;
Mitchell, JK ;
Lafitte, D ;
Briand, C ;
Derrick, PJ ;
Barras, F .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (52) :48915-48920
[6]   Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase [J].
Kryukov, GV ;
Kumar, RA ;
Koc, A ;
Sun, ZH ;
Gladyshev, VN .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (07) :4245-4250
[7]   Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme [J].
Lowther, WT ;
Brot, N ;
Weissbach, H ;
Matthews, BW .
BIOCHEMISTRY, 2000, 39 (44) :13307-13312
[8]   The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB [J].
Lowther, WT ;
Weissbach, H ;
Etienne, F ;
Brot, N ;
Matthews, BW .
NATURE STRUCTURAL BIOLOGY, 2002, 9 (05) :348-352
[9]   Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity [J].
Moskovitz, J ;
Singh, VK ;
Requena, J ;
Wilkinson, BJ ;
Jayaswal, RK ;
Stadtman, ER .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2002, 290 (01) :62-65
[10]   Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens [J].
Nathan, C ;
Shiloh, MU .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (16) :8841-8848