| Title : Crystal structure of cutinase Est119 from Thermobifida alba AHK119 that can degrade modified polyethylene terephthalate at 1.76A resolution - Kitadokoro_2012_Polym.Degrad.Stab_97_771 |
| Author(s) : Kitadokoro K , Thumarat U , Nakamura R , Nishimura K , Karatani H , Suzuki H , Kawai F |
| Ref : Polymer Degradation and Stability , 97 :771 , 2012 |
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Abstract :
We determined the crystal structure of a cutinase from Thermobifida alba AHK119 (Est119) at a resolution of 1.76A. The overall structure of Est119 displays a typical alpha/beta-hydrolase fold consisting of a central twisted beta-sheet of nine beta-strands that are flanked by nine alpha-helices on both sides. The refined model contains two monomers in the asymmetric unit that form a dimer interface; a polyethylene glycol fragment is bound in the interface. Polyethylene glycol-binding site on the protein may suggest a glycol-binding site. A putative polymer-recognizing groove is observed to continue through the catalytic pocket. Water molecules are bound to hydrophilic amino acids along the groove, indicating the alternating pattern of polar and hydrophobic residues. |
| PubMedSearch : Kitadokoro_2012_Polym.Degrad.Stab_97_771 |
| PubMedID: |
| Gene_locus related to this paper: 9acto-f7ix06 |
| Inhibitor | PEG-4000 |
| Substrate | HEMT Polyethylene-terephthalate |
| Gene_locus | 9acto-f7ix06 |
| Family | Polyesterase-lipase-cutinase |
| Structure | 3WYN 3VIS |
Kitadokoro K, Thumarat U, Nakamura R, Nishimura K, Karatani H, Suzuki H, Kawai F (2012)
Crystal structure of cutinase Est119 from Thermobifida alba AHK119 that can degrade modified polyethylene terephthalate at 1.76A resolution
Polymer Degradation and Stability
97 :771
Kitadokoro K, Thumarat U, Nakamura R, Nishimura K, Karatani H, Suzuki H, Kawai F (2012)
Polymer Degradation and Stability
97 :771