Crystallization and preliminary X-ray crystallographic analysis of a<i>yedU</i>gene product from<i>Escherichia coli</i>

Kim, Ok Gwan; Kim, In Kwon; Kim, Ghyung Hwa; Ko, Jong Soo; Park, Chankyu; Suh, Pann Ghill; Kang, Shinjae; Lee, Heung Soo; Shin, Sun Mi

doi:10.1107/s0907444902007369

Cited by 4 publications

(11 citation statements)

References 28 publications

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“…Structural alignment of EcHsp31 and PhPI (Fig. 6) results in 19% sequence identity, which is much lower than the 25.9% reported on the basis of sequence alone (9). Fig.…”

Section: Resultsmentioning

confidence: 72%

“…Sequence similarities have previously been identified between EcHsp31 and PfPI, another member of the DJ-1͞PfPI family (9). Together, PfPI and PhPI make up class III orthologs with Ͻ20% sequence identity to EcHsp31.…”

Section: Resultsmentioning

confidence: 92%

“…Recently, we have shown that E. coli Hsp31 (EcHsp31), the stress-inducible (6) and H-NS-regulated (7) product of the yedU gene (now referred to as hchA for heat-inducible chaperone), is an efficient homodimeric molecular chaperone whose activity is modulated by temperature and ATP binding (8). While highly conserved orthologs of unknown function are present in a number of pathogenic eubacteria and fungi (8), EcHsp31 also shares Ϸ19% identity with Pyrococcus horikoshii protease I (PhPI) (9) and contains a signature sequence matching that of the ␣-␤ hydrolases (10). In an effort to gain further insight on EcHsp31 function, we determined its structure at 1.6-Å resolution.…”

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confidence: 99%

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The 1.6-Å crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad

Quigley

Korotkov

Baneyx

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

102

139

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Heat shock proteins (Hsps) play essential protective roles under stress conditions by preventing the formation of protein aggregates and degrading misfolded proteins. EcHsp31, the yedU (hchA) gene product, is a representative member of a family of chaperones that alleviates protein misfolding by interacting with early unfolding intermediates. The 1.6-Å crystal structure of the EcHsp31 dimer reveals a system of hydrophobic patches, canyons, and grooves, which may stabilize partially unfolded substrate. The presence of a well conserved, yet buried, triad in each two-domain subunit suggests a still unproven hydrolytic function of the protein. A flexible extended linker between the A and P domains may play a role in conformational flexibility and substrate binding. The ␣-␤ sandwich of the EcHsp31 monomer shows structural similarity to PhPI, a protease belonging to the DJ-1 superfamily. The structure-guided sequence alignment indicates that Hsp31 homologs can be divided in three classes based on variations in the P domain that dramatically affect both oligomerization and catalytic triad formation.heat shock protein ͉ Pyrococcus horikoshii protease I (PhPI) ͉ DJ-1 family

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“…Structural alignment of EcHsp31 and PhPI (Fig. 6) results in 19% sequence identity, which is much lower than the 25.9% reported on the basis of sequence alone (9). Fig.…”

Section: Resultsmentioning

confidence: 72%

Section: Resultsmentioning

confidence: 92%

mentioning

confidence: 99%

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The 1.6-Å crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad

Quigley

Korotkov

Baneyx

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

102

139

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“…The previously reported orthorhombic crystals of Hsp31 (16) were not reproducible. Therefore, we found a new crystallization condition.…”

mentioning

confidence: 87%

Crystal Structures of Human DJ-1 and Escherichia coli Hsp31, Which Share an Evolutionarily Conserved Domain

Lee

Kim

et al. 2003

Journal of Biological Chemistry

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228

242

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Human DJ-1 and Escherichia coli Hsp31 belong to ThiJ/PfpI family, whose members contain a conserved domain. DJ-1 is associated with autosomal recessive early onset parkinsonism and Hsp31 is a molecular chaperone. Structural comparisons between DJ-1, Hsp31, and an Archaea protease, a member of ThiJ/PfpI family, lead to the identification of the chaperone activity of DJ-1 and the proteolytic activity of Hsp31. Moreover, the comparisons provide insights into how the functional diversity is realized in proteins that share an evolutionarily conserved domain. On the basis of the chaperone activity the possible role of DJ-1 in the pathogenesis of Parkinson's disease is discussed.

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“…8,20,21 Recently, we identified a soluble NAD(P)Hdependent quinone oxidoreductase (QOR2), the 30-kDa product of the ytfG gene, from E. coli. 22 QOR2, like ζ-crystallin-type oxidoreductases, requires no prosthetic group for the catalysis. However, there are several remarkable differences between QOR2 and ζ-crystallin-type oxidoreductases.…”

Section: Introductionmentioning

confidence: 99%

Crystal Structure of a New Type of NADPH-Dependent Quinone Oxidoreductase (QOR2) from Escherichia coli

Kim

Yim

Kim

et al. 2008

Journal of Molecular Biology

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Crystallization and preliminary X-ray crystallographic analysis of ayedUgene product fromEscherichia coli

Cited by 4 publications

References 28 publications

The 1.6-Å crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad

The 1.6-Å crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad

Crystal Structures of Human DJ-1 and Escherichia coli Hsp31, Which Share an Evolutionarily Conserved Domain

Crystal Structure of a New Type of NADPH-Dependent Quinone Oxidoreductase (QOR2) from Escherichia coli

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