Literature DB >> 20057071

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

Young Jun An1, Chang-Ro Lee, Supangat Supangat, Hyun Sook Lee, Jung-Hyun Lee, Sung Gyun Kang, Sun-Shin Cha.   

Abstract

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 A 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 A. Assuming the presence of two monomers in the asymmetric unit, the solvent content was estimated to be about 60.7%.

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Year:  2009        PMID: 20057071      PMCID: PMC2805537          DOI: 10.1107/S1744309109048039

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  24 in total

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Journal:  Science       Date:  1999-12-03       Impact factor: 47.728

2.  The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site.

Authors:  Istvan Botos; Edward E Melnikov; Scott Cherry; Joseph E Tropea; Anna G Khalatova; Fatima Rasulova; Zbigniew Dauter; Michael R Maurizi; Tatyana V Rotanova; Alexander Wlodawer; Alla Gustchina
Journal:  J Biol Chem       Date:  2003-12-09       Impact factor: 5.157

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Authors:  A L Goldberg
Journal:  Eur J Biochem       Date:  1992-01-15

4.  Mg2+-linked oligomerization modulates the catalytic activity of the Lon (La) protease from Mycobacterium smegmatis.

Authors:  S G Rudyak; M Brenowitz; T E Shrader
Journal:  Biochemistry       Date:  2001-08-07       Impact factor: 3.162

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Authors:  J D Kowit; A L Goldberg
Journal:  J Biol Chem       Date:  1977-12-10       Impact factor: 5.157

6.  Solvent content of protein crystals.

Authors:  B W Matthews
Journal:  J Mol Biol       Date:  1968-04-28       Impact factor: 5.469

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Authors:  K H Swamy; A L Goldberg
Journal:  Nature       Date:  1981-08-13       Impact factor: 49.962

8.  The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.

Authors:  Hyun Sook Lee; Sung Gyun Kang; Seung Seob Bae; Jae Kyu Lim; Yona Cho; Yun Jae Kim; Jeong Ho Jeon; Sun-Shin Cha; Kae Kyoung Kwon; Hyung-Tae Kim; Cheol-Joo Park; Hee-Wook Lee; Seung Il Kim; Jongsik Chun; Rita R Colwell; Sang-Jin Kim; Jung-Hyun Lee
Journal:  J Bacteriol       Date:  2008-09-12       Impact factor: 3.490

9.  A membrane-bound archaeal Lon protease displays ATP-independent proteolytic activity towards unfolded proteins and ATP-dependent activity for folded proteins.

Authors:  Toshiaki Fukui; Tomohiro Eguchi; Haruyuki Atomi; Tadayuki Imanaka
Journal:  J Bacteriol       Date:  2002-07       Impact factor: 3.490

Review 10.  Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution.

Authors:  Istvan Botos; Edward E Melnikov; Scott Cherry; Anna G Khalatova; Fatima S Rasulova; Joseph E Tropea; Michael R Maurizi; Tatyana V Rotanova; Alla Gustchina; Alexander Wlodawer
Journal:  J Struct Biol       Date:  2004 Apr-May       Impact factor: 2.867

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  2 in total

1.  Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber.

Authors:  Sun-Shin Cha; Young Jun An; Chang Ro Lee; Hyun Sook Lee; Yeon-Gil Kim; Sang Jin Kim; Kae Kyoung Kwon; Gian Marco De Donatis; Jung-Hyun Lee; Michael R Maurizi; Sung Gyun Kang
Journal:  EMBO J       Date:  2010-09-10       Impact factor: 11.598

2.  Structural basis for the ATP-independent proteolytic activity of LonB proteases and reclassification of their AAA+ modules.

Authors:  Young Jun An; Jung-Hyun Na; Myung-Il Kim; Sun-Shin Cha
Journal:  J Microbiol       Date:  2015-10-02       Impact factor: 3.422

  2 in total

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