3H18
Crystal structure of EstE5-PMSF (II)
Summary for 3H18
| Entry DOI | 10.2210/pdb3h18/pdb |
| Related | 3FAK 3G9U 3G9V 3G9Z 3H17 3H19 3H1A 3H1B |
| Descriptor | Esterase/lipase, phenylmethanesulfonic acid (3 entities in total) |
| Functional Keywords | hsl, este5, esterase, lipase, hydrolase, pmsf, phenylmethylsulfonyl fluoride |
| Biological source | Uncultured bacterium |
| Total number of polymer chains | 1 |
| Total formula weight | 34992.33 |
| Authors | Hwang, K.Y.,Nam, K.H. (deposition date: 2009-04-11, release date: 2009-04-28, Last modification date: 2024-11-13) |
| Primary citation | Nam, K.H.,Kim, S.J.,Priyadarshi, A.,Kim, H.S.,Hwang, K.Y. The crystal structure of an HSL-homolog EstE5 complex with PMSF reveals a unique configuration that inhibits the nucleophile Ser144 in catalytic triads. Biochem.Biophys.Res.Commun., 389:247-250, 2009 Cited by PubMed Abstract: The esterase/lipase family (EC 3.1.1.3/EC 3.1.1.1) represents a diverse group of hydrolases that catalyze the cleavage of ester bonds and are widely distributed in animals, plants and microorganisms. Among these enzymes, hormone-sensitive lipases, play a critical role in the regulation of rodent fat cell lipolysis and are regarded as adipose tissue-specific enzymes. Recently, we reported the structural and biological characterization of EstE5 from the metagenome library [K.H. Nam, M.Y. Kim, S.J. Kim, A. Priyadarshi, W.H. Lee, K.Y. Hwang, Structural and functional analysis of a novel EstE5 belonging to the subfamily of hormone-sensitive lipase, Biochem. Biophys. Res. Commun. 379 (2009) 553-556]. The structure of this protein revealed that it belongs to the HSL-family. Here, we report the inhibition of the activity of the HSL-homolog EstE5 protein as determined by the use of esterase/lipase inhibitors. Our results revealed that the EstE5 protein is significantly inhibited by PMSF. In addition, this is the first study to identify the crystal structures of EstE5-PMSF at 2.4 and 2.5A among the HSL-homolog structures. This structural configuration is similar to that adopted when serine proteases are inhibited by PMSF. The results presented here provide valuable information regarding the properties of the HSL-family. PubMed: 19715665DOI: 10.1016/j.bbrc.2009.08.123 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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