Crystal structure of Hsp33 chaperone (TM1394) from Thermotoga maritima at 2.20 Å resolution

被引:12
作者
Jaroszewski, L
Schwarzenbacher, R
McMullan, D
Abdubek, P
Agarwalla, S
Ambing, E
Axelrod, H
Biorac, T
Canaves, JM
Chiu, HJ
Deacon, AM
DiDonato, M
Elsliger, MA
Godzik, A
Grittini, C
Grzechnik, SK
Hale, J
Hampton, E
Han, GW
Haugen, J
Hornsby, M
Klock, HE
Koesema, E
Kreusch, A
Kuhn, P
Lesley, SA
Miller, MD
Moy, K
Nigoghossian, E
Paulsen, J
Quijano, K
Reyes, R
Rife, C
Spraggon, G
Stevens, RC
van den Bedem, H
Velasquez, J
Vincent, J
White, A
Wolf, G
Xu, QP
Hodgson, KO
Wooley, J
Wilson, IA
机构
[1] Scripps Res Inst, La Jolla, CA 92037 USA
[2] Stanford Univ, Stanford Synchrotron Radiat Lab, Menlo Pk, CA USA
[3] Univ Calif San Diego, La Jolla, CA 92093 USA
[4] Novartis Res Fdn, Genom Inst, San Diego, CA USA
关键词
D O I
10.1002/prot.20542
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
[No abstract available]
引用
收藏
页码:669 / 673
页数:5
相关论文
共 16 条
[1]   THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].
BAILEY, S .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 :760-763
[2]   Activation of the redox-regulated chaperone Hsp33 by domain unfolding [J].
Graf, PCF ;
Martinez-Yamout, M ;
VanHaerents, S ;
Lilie, H ;
Dyson, HJ ;
Jakob, U .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (19) :20529-20538
[3]   DALI - A NETWORK TOOL FOR PROTEIN-STRUCTURE COMPARISON [J].
HOLM, L ;
SANDER, C .
TRENDS IN BIOCHEMICAL SCIENCES, 1995, 20 (11) :478-480
[4]   Chaperone activity with a redox switch [J].
Jakob, U ;
Muse, W ;
Eser, M ;
Bardwell, JCA .
CELL, 1999, 96 (03) :341-352
[5]   The crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism [J].
Janda, I ;
Devedjiev, Y ;
Derewenda, U ;
Dauter, Z ;
Bielnicki, J ;
Cooper, DR ;
Graf, PCF ;
Joachimiak, A ;
Jakob, U ;
Derewenda, ZS .
STRUCTURE, 2004, 12 (10) :1901-1907
[6]   IMPROVED METHODS FOR BUILDING PROTEIN MODELS IN ELECTRON-DENSITY MAPS AND THE LOCATION OF ERRORS IN THESE MODELS [J].
JONES, TA ;
ZOU, JY ;
COWAN, SW ;
KJELDGAARD, M .
ACTA CRYSTALLOGRAPHICA SECTION A, 1991, 47 :110-119
[7]   Crystal structure of proteolytic fragments of the redox-sensitive Hsp33 with constitutive chaperone activity [J].
Kim, SJ ;
Jeong, DG ;
Chi, SW ;
Lee, JS ;
Ryu, SE .
NATURE STRUCTURAL BIOLOGY, 2001, 8 (05) :459-466
[8]   Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline [J].
Lesley, SA ;
Kuhn, P ;
Godzik, A ;
Deacon, AM ;
Mathews, I ;
Kreusch, A ;
Spraggon, G ;
Klock, HE ;
McMullan, D ;
Shin, T ;
Vincent, J ;
Robb, A ;
Brinen, LS ;
Miller, MD ;
McPhillips, TM ;
Miller, MA ;
Scheibe, D ;
Canaves, JM ;
Guda, C ;
Jaroszewski, L ;
Selby, TL ;
Elsliger, MA ;
Wooley, J ;
Taylor, SS ;
Hodgson, KO ;
Wilson, IA ;
Schultz, PG ;
Stevens, RC .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (18) :11664-11669
[9]  
Leslie AGW., 1992, JOINT CCP4 ESF EAMCB, P26
[10]   Structure validation by Cα geometry:: φ,ψ and Cβ deviation [J].
Lovell, SC ;
Davis, IW ;
Adrendall, WB ;
de Bakker, PIW ;
Word, JM ;
Prisant, MG ;
Richardson, JS ;
Richardson, DC .
PROTEINS-STRUCTURE FUNCTION AND GENETICS, 2003, 50 (03) :437-450