[https://www.uniprot.org/uniprot/PHAZ_TALFU PHAZ_TALFU] Esterase involved in the hydrolysis of polyhydroxybutyrate, a microbial polyester that can be produced from renewable resources.<ref>PMID:16405909</ref> <ref>PMID:1929416</ref> [PROSITE-ProRule:PRU00498]
2d80 is a 1 chain structure with sequence from Talaromyces funiculosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
PHAZ_TALFU Esterase involved in the hydrolysis of polyhydroxybutyrate, a microbial polyester that can be produced from renewable resources.[1][2] [PROSITE-ProRule:PRU00498]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Polyhydroxybutyrate is a microbial polyester that can be produced from renewable resources, and is degraded by the enzyme polyhydroxybutyrate depolymerase. The crystal structures of polyhydroxybutyrate depolymerase from Penicillium funiculosum and its S39 A mutant complexed with the methyl ester of a trimer substrate of (R)-3-hydroxybutyrate have been determined at resolutions of 1.71 A and 1.66 A, respectively. The enzyme is comprised of a single domain, which represents a circularly permuted variant of the alpha/beta hydrolase fold. The catalytic residues Ser39, Asp121, and His155 are located at topologically conserved positions. The main chain amide groups of Ser40 and Cys250 form an oxyanion hole. A crevice is formed on the surface of the enzyme, to which a single polymer chain can be bound by predominantly hydrophobic interactions with several hydrophobic residues. The structure of the S39A mutant-trimeric substrate complex reveals that Trp307 is responsible for the recognition of the ester group adjacent to the scissile group. It is also revealed that the substrate-binding site includes at least three, and possibly four, subsites for binding monomer units of polyester substrates. Thirteen hydrophobic residues, which are exposed to solvent, are aligned around the mouth of the crevice, forming a putative adsorption site for the polymer surface. These residues may contribute to the sufficient binding affinity of the enzyme for PHB granules without a distinct substrate-binding domain.
The crystal structure of polyhydroxybutyrate depolymerase from Penicillium funiculosum provides insights into the recognition and degradation of biopolyesters.,Hisano T, Kasuya K, Tezuka Y, Ishii N, Kobayashi T, Shiraki M, Oroudjev E, Hansma H, Iwata T, Doi Y, Saito T, Miki K J Mol Biol. 2006 Mar 3;356(4):993-1004. Epub 2005 Dec 27. PMID:16405909[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Hisano T, Kasuya K, Tezuka Y, Ishii N, Kobayashi T, Shiraki M, Oroudjev E, Hansma H, Iwata T, Doi Y, Saito T, Miki K. The crystal structure of polyhydroxybutyrate depolymerase from Penicillium funiculosum provides insights into the recognition and degradation of biopolyesters. J Mol Biol. 2006 Mar 3;356(4):993-1004. Epub 2005 Dec 27. PMID:16405909 doi:10.1016/j.jmb.2005.12.028
↑Brucato CL, Wong SS. Extracellular poly(3-hydroxybutyrate) depolymerase from Penicillium funiculosum: general characteristics and active site studies. Arch Biochem Biophys. 1991 Nov 1;290(2):497-502. PMID:1929416 doi:10.1016/0003-9861(91)90572-z
↑Hisano T, Kasuya K, Tezuka Y, Ishii N, Kobayashi T, Shiraki M, Oroudjev E, Hansma H, Iwata T, Doi Y, Saito T, Miki K. The crystal structure of polyhydroxybutyrate depolymerase from Penicillium funiculosum provides insights into the recognition and degradation of biopolyesters. J Mol Biol. 2006 Mar 3;356(4):993-1004. Epub 2005 Dec 27. PMID:16405909 doi:10.1016/j.jmb.2005.12.028
