5AOB: The Structure Of A Novel Thermophilic Esterase From The Planctomycetes Species, Thermogutta Terrifontis, Est2-butyrate Bound

Citation:
Abstract
A carboxyl esterase (TtEst2) has been identified in a novel thermophilic bacterium, Thermogutta terrifontis from the phylum Planctomycetes and has been cloned and over-expressed in Escherichia coli. The enzyme has been characterized biochemically and shown to have activity toward small p-nitrophenyl (pNP) carboxylic esters with optimal activity for pNP-acetate. The enzyme shows moderate thermostability retaining 75% activity after incubation for 30 min at 70 degrees C. The crystal structures have been determined for the native TtEst2 and its complexes with the carboxylic acid products propionate, butyrate, and valerate. TtEst2 differs from most enzymes of the alpha/beta-hydrolase family 3 as it lacks the majority of the 'cap' domain and its active site cavity is exposed to the solvent. The bound ligands have allowed the identification of the carboxyl pocket in the enzyme active site. Comparison of TtEst2 with structurally related enzymes has given insight into how differences in their substrate preference can be rationalized based upon the properties of their active site pockets.
PDB ID: 5AOBDownload
MMDB ID: 134686
PDB Deposition Date: 2015/9/10
Updated in MMDB: 2015/12
Experimental Method:
x-ray diffraction
Resolution: 1.79  Å
Source Organism:
Similar Structures:
Biological Unit for 5AOB: monomeric; determined by author and by software (PISA)
Molecular Components in 5AOB
Label Count Molecule
Protein (1 molecule)
1
Esterase
Molecule annotation
Chemicals (10 molecules)
1
2
2
1
3
4
4
1
5
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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