Crystallization and preliminary X-ray crystallographic analysis of Lon from Thermococcus onnurineus NA1

被引：3
作者：
An, Young Jun [1 ,2 ]
Lee, Chang-Ro [1 ]
Supangat, Supangat [1 ]
Lee, Hyun Sook [1 ]
Lee, Jung-Hyun [1 ,3 ]
Kang, Sung Gyun [1 ,3 ]
Cha, Sun-Shin [1 ,3 ]
机构：
[1] Korea Ocean Res & Dev Inst, Marine Biotechnol Res Ctr, Ansan 426744, South Korea
[2] Myongji Univ, Dept Biol Sci, Yongin 449728, South Korea
[3] Univ Sci & Technol, Dept Marine Biotechnol, Taejon 305333, South Korea
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷
关键词：
ATP-DEPENDENT PROTEASE; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; PROTEOLYTIC DOMAIN; QUALITY-CONTROL; ACTIVE-SITE; RESOLUTION; BACTERIAL; PROTEINS; REVEALS;
D O I：
10.1107/S1744309109048039
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Lon is an oligomeric ATP-dependent protease that degrades defective or denatured proteins as well as some folded proteins for the control of cellular protein quality and metabolism. Lon from Thermococcus onnurineus NA1 was purified and crystallized at 295 K. A 2.0 angstrom resolution data set was collected using synchrotron radiation. The crystals belonged to space group P6(3), with unit-cell parameters a = 121.45, b = 121.45, c = 195.24 angstrom. Assuming the presence of two monomers in the asymmetric unit, the solvent content was estimated to be about 60.7%.
引用
收藏
页码：54 / 56
页数：3
相关论文
共 25 条
  • [1] ATP-dependent proteases of bacteria: recognition logic and operating principles
    Baker, Tania A.
    Sauer, Robert T.
    [J]. TRENDS IN BIOCHEMICAL SCIENCES, 2006, 31 (12) : 647 - 653
  • [2] Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus Lon reveals the conformational variability in the active sites of Lon proteases
    Botos, I
    Melnikov, EE
    Cherry, S
    Kozov, S
    Makhovskaya, OV
    Tropea, JE
    Gustchina, A
    Rotanova, TV
    Wlodawer, A
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2005, 351 (01) : 144 - 157
  • [3] Crystal structure of the AAA+ α domain of E-coli Lon protease at 1.9Å resolution
    Botos, I
    Melnikov, EE
    Cherry, S
    Khalatova, AG
    Rasulova, FS
    Tropea, JE
    Maurizi, MR
    Rotanova, TV
    Gustchina, A
    Wlodawer, A
    [J]. JOURNAL OF STRUCTURAL BIOLOGY, 2004, 146 (1-2) : 113 - 122
  • [4] The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site
    Botos, I
    Melnikov, EE
    Cherry, S
    Tropea, JE
    Khalatova, AG
    Rasulova, F
    Dauter, Z
    Maurizi, MR
    Rotanova, TV
    Wlodawer, A
    Gustchina, A
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (09) : 8140 - 8148
  • [5] A membrane-bound archaeal lon protease displays ATP-independent proteolytic activity towards unfolded proteins and ATP-dependent activity for folded proteins
    Fukui, T
    Eguchi, T
    Atomi, H
    Imanaka, T
    [J]. JOURNAL OF BACTERIOLOGY, 2002, 184 (13) : 3689 - 3698
  • [6] GOLDBERG AL, 1994, METHOD ENZYMOL, V244, P350
  • [7] THE MECHANISM AND FUNCTIONS OF ATP-DEPENDENT PROTEASES IN BACTERIAL AND ANIMAL-CELLS
    GOLDBERG, AL
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1992, 203 (1-2): : 9 - 23
  • [8] Protein quality control: Triage by chaperones and proteases
    Gottesman, S
    Wickner, S
    Maurizi, MR
    [J]. GENES & DEVELOPMENT, 1997, 11 (07) : 815 - 823
  • [9] The active site of a Lon protease from Methanococcus jannaschii distinctly differs from the canonical catalytic dyad of Lon proteases
    Im, YJ
    Na, Y
    Kang, GB
    Rho, SH
    Kim, MK
    Lee, JH
    Chung, CH
    Eom, SH
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (51) : 53451 - 53457
  • [10] KOWIT JD, 1977, J BIOL CHEM, V252, P8350
123