Crystallization and Preliminary X-ray Crystallographic Analysis of a 40 kDa N-Terminal Fragment of the Yeast Prion-Remodeling Factor Hsp104

doi:10.1107/S1744309107038328

Title: Crystallization and Preliminary X-ray Crystallographic Analysis of a 40 kDa N-Terminal Fragment of the Yeast Prion-Remodeling Factor Hsp104

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Abstract

A 40 kDa N-terminal fragment of Saccharomyces cerevisiae Hsp104 was crystallized in two different crystal forms. Native 1 diffracted to 2.6 {angstrom} resolution and belonged to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 66.6, b = 75.8, c = 235.7 {angstrom}. Native 2 diffracted to 2.9 {angstrom} resolution and belonged to space group P6{sub 1}22 or P6{sub 5}22, with unit-cell parameters a = 179.1, b = 179.1, c = 69.7 {angstrom}. This is the first report of the crystallization of a eukaryotic member of the Hsp100 family of molecular chaperones.

Authors:: Lee,S.; Tsai, F.

Publication Date:: Mon Jan 01 00:00:00 EST 2007

Research Org.:: Brookhaven National Laboratory (BNL) National Synchrotron Light Source

Sponsoring Org.:: Doe - Office Of Science

OSTI Identifier:: 930006

Report Number(s):: BNL-80619-2008-JA
TRN: US200822%%957

DOE Contract Number:: DE-AC02-98CH10886

Resource Type:: Journal Article

Resource Relation:: Journal Name: Acta Crystallographica Section F: Structural Biology and Crystallization Communications; Journal Volume: 63

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; CRYSTALLIZATION; CRYSTALS; RESOLUTION; SACCHAROMYCES CEREVISIAE; SPACE GROUPS; YEASTS; X-RAY DIFFRACTION; national synchrotron light source

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                    Lee,S., and Tsai, F.. Crystallization and Preliminary X-ray Crystallographic Analysis of a 40 kDa N-Terminal Fragment of the Yeast Prion-Remodeling Factor Hsp104.  United States: N. p., 2007. 
        Web.  doi:10.1107/S1744309107038328.

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                    Lee,S., & Tsai, F.. Crystallization and Preliminary X-ray Crystallographic Analysis of a 40 kDa N-Terminal Fragment of the Yeast Prion-Remodeling Factor Hsp104.  United States.  doi:10.1107/S1744309107038328.

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                    Lee,S., and Tsai, F.. Mon .  
        "Crystallization and Preliminary X-ray Crystallographic Analysis of a 40 kDa N-Terminal Fragment of the Yeast Prion-Remodeling Factor Hsp104".  United States.  
        doi:10.1107/S1744309107038328.

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@article{osti_930006,

  title        = {Crystallization and Preliminary X-ray Crystallographic Analysis of a 40 kDa N-Terminal Fragment of the Yeast Prion-Remodeling Factor Hsp104},

  author       = {Lee,S. and Tsai, F.},

  abstractNote = {A 40 kDa N-terminal fragment of Saccharomyces cerevisiae Hsp104 was crystallized in two different crystal forms. Native 1 diffracted to 2.6 {angstrom} resolution and belonged to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 66.6, b = 75.8, c = 235.7 {angstrom}. Native 2 diffracted to 2.9 {angstrom} resolution and belonged to space group P6{sub 1}22 or P6{sub 5}22, with unit-cell parameters a = 179.1, b = 179.1, c = 69.7 {angstrom}. This is the first report of the crystallization of a eukaryotic member of the Hsp100 family of molecular chaperones.},

  doi          = {10.1107/S1744309107038328},

  journal      = {Acta Crystallographica Section F: Structural Biology and Crystallization Communications},

  number       = ,

  volume       = 63,

  place        = {United States},

  year         = {Mon Jan 01 00:00:00 EST 2007},

  month        = {Mon Jan 01 00:00:00 EST 2007}

}

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DOI: 10.1107/S1744309107038328

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Crystallization and preliminary X-ray crystallographic analysis of a 40 kDa N-terminal fragment of the yeast prion-remodeling factor Hsp104

Lee, Sukyeong ; Tsai, Francis T. F., E-mail: ftsai@bcm.tmc.edu - Acta Crystallographica. Section F

An N-terminal fragment of S. cerevisiae Hsp104 has been crystallized. This is the first report of the crystallization of a eukaryotic member of the Hsp100 family of molecular chaperones. A 40 kDa N-terminal fragment of Saccharomyces cerevisiae Hsp104 was crystallized in two different crystal forms. Native 1 diffracted to 2.6 Å resolution and belonged to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 66.6, b = 75.8, c = 235.7 Å. Native 2 diffracted to 2.9 Å resolution and belonged to space group P6{sub 1}22 or P6{sub 5}22, with unit-cell parameters a = 179.1, b = 179.1,more »« less
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The crystallization and preliminary X-ray crystallographic studies of the N-terminal domain of FadD28, a fatty-acyl AMP ligase from M. tuberculosis, are reported. FadD28 from Mycobacterium tuberculosis belongs to the fatty-acyl AMP ligase (FAAL) family of proteins. It is essential for the biosynthesis of a virulent phthiocerol dimycocerosate (PDIM) lipid that is only found in the cell wall of pathogenic mycobacteria. The N-terminal domain, comprising of the first 460 residues, was crystallized by the hanging-drop vapour-diffusion method at 295 K. The crystals belong to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 50.97, b = 60.74, c =more »« less
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An N-terminal acetyltransferase ARD1 subunit-related protein (Ta0058) and an N-terminal acetyltransferase-related protein (Ta1140) from T. acidophilum were crystallized. X-ray diffraction data were collected to 2.17 and 2.40 Å, respectively. N-terminal acetylation is one of the most common protein modifications in eukaryotes, occurring in approximately 80–90% of cytosolic mammalian proteins and about 50% of yeast proteins. ARD1 (arrest-defective protein 1), together with NAT1 (N-acetyltransferase protein 1) and possibly NAT5, is responsible for the NatA activity in Saccharomyces cerevisiae. In mammals, ARD1 is involved in cell proliferation, neuronal development and cancer. Interestingly, it has been reported that mouse ARD1 (mARD1{sup 225}) mediatesmore »« less
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Yeast NAD{sup +}-isocitrate dehydrogenase has been purified and crystallized using sodium citrate, a competitive inhibitor of the enzyme, as a precipitant. Preliminary X-ray analyses indicate the molecular boundaries of the molecule and large continuous solvent channels in the crystal. NAD{sup +}-specific isocitrate dehydrogenase (IDH; EC 1.1.1.41) is a complex allosterically regulated enzyme in the tricarboxylic acid cycle. Yeast IDH is believed to be an octamer containing four catalytic IDH2 and four regulatory IDH1 subunits. Crystals of yeast IDH have been obtained and optimized using sodium citrate, a competitive inhibitor of the enzyme, as the precipitating agent. The crystals belong tomore »« less
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Crystallization and preliminary X-ray crystallographic analysis of the Escherichia coli outer membrane cobalamin transporter BtuB in complex with the carboxy-terminal domain of TonB

Shultis, David D. ; Purdy, Michael D. ; Banchs, Christian N. ; ... - Acta Crystallographica. Section F

Crystals of a complex of the E. coli proteins BtuB (outer membrane cobalamin transporter) and TonB (carboxy-terminal domain) diffracting to 2.1 Å resolution have been obtained. The energy-dependent uptake of organometallic compounds and other micronutrients across the outer membranes of Gram-negative bacteria is carried out by outer membrane active-transport proteins that utilize the proton-motive force of the inner membrane via coupling to the TonB protein. The Escherichia coli outer membrane cobalamin transporter BtuB and a carboxy-terminal domain of the TonB protein, residues 147–239 of the wild-type protein, were expressed and purified individually. A complex of BtuB and TonB{sup 147–239} wasmore »« less
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