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PDB ID 2pzh

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2pzh, resolution 1.70Å ()
Gene: HP0496 (Helicobacter pylori)
Related: 1lo7, 1s5u
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml

YbgCis believed to have first appeared in the Tol complex with the separation of the δε proteobacteria from the αβγ proteobacteria[1].


YbgC is a cytoplasmic protein in the Tol-Pal complex[2]. In Helicobacter pylori, the protein is part of a 'hot-dog' family of proteins, with an epsilongamma tetrameric arrangement[3].


The protein displays thioesterase activity towards acyl-CoA thioesters[3], and has a strong sequence conservation with its active site residues with other proteins of a similar function[4] for example with the Pseudonomas sp. strain CBS3 4-hydroxybenzoyl-CoA thioesterase[5].

However, its role within the Tol complex itself remains unknown, although it may be involved in the acetylation of another protein within the complex, with the role of an activity-regulator[1]. It is also thought to be involved in the cell division complex of Tol-Pal[3].


  1. 1.0 1.1 Sturgis JN. Organisation and evolution of the tol-pal gene cluster. J Mol Microbiol Biotechnol. 2001 Jan;3(1):113-22. PMID:11200223
  2. Walburger A, Lazdunski C, Corda Y. The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB. Mol Microbiol. 2002 May;44(3):695-708. PMID:11994151
  3. 3.0 3.1 3.2 Angelini A, Cendron L, Goncalves S, Zanotti G, Terradot L. Structural and enzymatic characterization of HP0496, a YbgC thioesterase from Helicobacter pylori. Proteins. 2008 Mar 12;72(4):1212-1221. PMID:18338382 doi:http://dx.doi.org/10.1002/prot.22014
  4. Benning MM, Wesenberg G, Liu R, Taylor KL, Dunaway-Mariano D, Holden HM. The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. Strain CBS-3. J Biol Chem. 1998 Dec 11;273(50):33572-9. PMID:9837940
  5. Zhuang Z, Song F, Martin BM, Dunaway-Mariano D. The YbgC protein encoded by the ybgC gene of the tol-pal gene cluster of Haemophilus influenzae catalyzes acyl-coenzyme A thioester hydrolysis. FEBS Lett. 2002 Apr 10;516(1-3):161-3. PMID:11959124

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