Crystal structure of a putative acyl‐CoA thioesterase from <i>Xanthomonas campestris</i> (XC229) adopts a tetrameric hotdog fold of ϵγ mode

Chin, Ko‐Hsin; Chou, Cheng‐Chun; Wang, Andrew H.‐J.; Chou, Shan‐Ho

doi:10.1002/prot.21037

Cited by 3 publications

(5 citation statements)

References 16 publications

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“…Structural genomics programs have shown that the crystal structures of conserved hypothetical protein YbaW (PDB codes: 1NJK from E. coli , 2ALI from P. aeruginosa , 2AV9 from P. aeruginosa , 2CYE from T. thermophilus , 2FUJ from X. campestris [ 40 ], 2NUJ from Jannaschia sp. CCS1 , 2OIW from B. stearothermophilus ) with the hot dog fold form tetramers of type TA similar to that of 4HBT-I.…”

Section: Resultsmentioning

confidence: 99%

Analysis of proteins with the 'hot dog' fold: Prediction of function and identification of catalytic residues of hypothetical proteins

et al. 2009

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Section: Resultsmentioning

confidence: 99%

Analysis of proteins with the 'hot dog' fold: Prediction of function and identification of catalytic residues of hypothetical proteins

et al. 2009

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“…strain CBS‐3 ( Ps HTE4) and from Arthrobacter sp . Strain SU ( Ar HTE5), the thioesterase II from E. coli ( Ec TEII6), the human thioesterase superfamily member 2 (hTHEM27), the putative acyl‐CoA thioesterase from Xanthomonas campestris (XC2298), the phenylacetate degradation protein PaaI from Thermus thermophilus ( Tt PaaI9), the YbgC protein from E. coli ( Ec YbgC; PDB ID code 1S5U), and two hypothetical proteins YbaW and YdiI from E. coli ( Ec YbaW; Ec YdiI10). These enzymes are all defined by the arrangement of two hot‐dog folds in γ dimers11 but these dimeric subunits form tetramers by two different modes.…”

Section: Introductionmentioning

confidence: 99%

Structural and enzymatic characterization of HP0496, a YbgC thioesterase from Helicobacter pylori

et al. 2008

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YbgC proteins are bacterial acyl-CoA thioesterases associated with the Tol-Pal system. This system is important for cell envelope integrity and is part of the cell division machinery. In E. coli, YbgC associates with the cell membrane and is part of a protein network involved in lipid biogenesis. In the human pathogen Helicobacter pylori, a putative homologue of YbgC, named HP0496, was found to interact with the cytotoxin CagA by two different studies. We have determined its crystal structure and characterized its enzymatic activity. The structure of HP0496 shows that it is a member of the hot-dog family of proteins, with a epsilongamma tetrameric arrangement. Finally, enzymatic assays performed with the purified protein showed that HP0496 is an acyl-CoA thioesterase that favors long-chain substrates.

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“…This orientation is called the " mode (Kunishima et al, 2005;Chin et al, 2006). This arrangement mode was also observed in 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas (PsHTE; Benning et al, 1998), the putative acyl-CoA thioesterase from X. campestris (XC229; Benning et al, 1998;Chin et al, 2006) and the bacterial acyl-CoA thioesterase HpYbgC from H. pylori (HP0496; Angelini et al, 2008). However, the tetramer orientations in TTHA1846 and HpYbgC are not the same.…”

Section: Overall Protein Structurementioning

confidence: 89%

“…The aminoacid sequence of XC229 is homologous to that of TTHA1846 (34% identity; Figs. 1a and 1b; Chin et al, 2006), but the largest differences between the TTHA1846 and XC229 thioesterases exist within the loop between 2 and 2 ( Fig. 7b).…”

Section: Putative Substratementioning

confidence: 98%

“…strain CBS-3 (PsHTE;Benning et al, 1998;Thoden et al, 2002) and from Arthrobacter sp. (ArHTE; Thoden et al, 2003), medium-chain acyl-CoA thioesterase II from E. coli (EcTEII; Li et al, 2000), TtPaaI from T. thermophilus (Kunishima et al, 2005), the putative acyl-CoA thioesterase from Xanthomonas campestris (XC229; Chin et al, 2006), human thioesterase superfamily member 2 (Cheng et al, 2006), acyl-CoA thioesterase from Haemophilus influenzae (HI0827; Willis et al, 2008) and the bacterial acyl-CoA thioesterase HpYbgC from Helicobacter pylori (Angelini et al, 2008). Here, we report the crystal structure of the thioesterasefamily member TTHA1846 from T. thermophilus HB8 in complex with CoA.…”

Section: Introductionmentioning

confidence: 99%

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Structure of the putative thioesterase protein TTHA1846 fromThermus thermophilusHB8 complexed with coenzyme A and a zinc ion

Hosaka¹,

Murayama

Kato-Murayama³

et al. 2009

Acta Crystallogr D Biol Cryst

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TTHA1846 is a conserved hypothetical protein from Thermus thermophilus HB8 with a molecular mass of 15.1 kDa that belongs to the thioesterase superfamily (Pfam 03061). Here, the 1.9 A resolution crystal structure of TTHA1846 from T. thermophilus is reported. The crystal structure is a dimer of dimers. Each subunit adopts the so-called hot-dog fold composed of five antiparallel beta-strands flanked on one side by a rather long alpha-helix and shares structural similarity to a number of thioesterases. Unexpectedly, TTHA1846 binds one metal ion and one ligand per subunit. The ligand density was modelled as coenzyme A (CoA). Its structure was confirmed by MALDI-TOF mass spectrometry and electron-density mapping. X-ray absorption fine-structure (XAFS) measurement of the crystal unambiguously characterized the metal ion as zinc. The zinc ion is tetrahedrally coordinated by the side chains of Asp18, His22 and Glu50 and the CoA thiol group. This is the first structural report of the interaction of CoA with a zinc ion. From structural and database analyses, it was speculated that the zinc ion may play an inhibitory role in the enzymatic activity.

show abstract

Crystal structure of a putative acyl‐CoA thioesterase from Xanthomonas campestris (XC229) adopts a tetrameric hotdog fold of ϵγ mode

Cited by 3 publications

References 16 publications

Analysis of proteins with the 'hot dog' fold: Prediction of function and identification of catalytic residues of hypothetical proteins

Analysis of proteins with the 'hot dog' fold: Prediction of function and identification of catalytic residues of hypothetical proteins

Structural and enzymatic characterization of HP0496, a YbgC thioesterase from Helicobacter pylori

Structure of the putative thioesterase protein TTHA1846 fromThermus thermophilusHB8 complexed with coenzyme A and a zinc ion

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