1qlw
THE ATOMIC RESOLUTION STRUCTURE OF A NOVEL BACTERIAL ESTERASE
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OverviewOverview
Background: A novel bacterial esterase that cleaves esters on halogenated, cyclic compounds has been isolated from an Alcaligenes species. This, esterase 713 is encoded by a 1062 base pair gene. The presence of a leader, sequence of 27 amino acids suggests that this enzyme is exported from the, cytosol. Esterase 713 has been over-expressed in Agrobacterium without, this leader sequence. Its amino acid sequence shows no significant, homology to any known protein sequence. Results: The crystal structure of, esterase 713 has been determined by multiple isomorphous replacement and, refined to 1. 1 A resolution. The subunits of this dimeric enzyme comprise, a single domain with an alpha/beta hydrolase fold. The catalytic triad has, been identified as Ser206-His298-Glu230. The acidic residue of ... [(full description)]
About this StructureAbout this Structure
1QLW is a [Single protein] structure of sequence from [Alcaligenes sp.] with SO4 as [ligand]. Structure known Active Sites: CS1 and CS2. Full crystallographic information is available from [OCA].
ReferenceReference
The atomic-resolution structure of a novel bacterial esterase., Bourne PC, Isupov MN, Littlechild JA, Structure. 2000 Feb 15;8(2):143-51. PMID:10673440
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