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Cloning, expression, purification and preliminary X-ray analysis of a putative metagenome-derived lipase.


ABSTRACT: LipS is a novel thermostable putative lipase that was isolated from a metagenomic library using functional screening methods. The corresponding gene shows high similarity to that encoding a putative but uncharacterized esterase from Symbiobacterium thermophilum IAM14863 (99% nucleotide-sequence similarity). Two different constructs of the recombinant lipase were crystallized. Crystals belonging to space group P4(2)2(1)2 diffracted X-ray radiation to 2.8 Å resolution and crystals belonging to space group P4 diffracted to 2.0 Å resolution. The most probable content of their asymmetric units were two molecules (P4(2)2(1)2) and four or five molecules (P4), respectively.

SUBMITTER: Fersini F 

PROVIDER: S-EPMC3412774 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature

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Cloning, expression, purification and preliminary X-ray analysis of a putative metagenome-derived lipase.

Fersini Francesco F   Dall'Antonia Yuliya Y   Chow Jennifer J   Streit Wolfgang R WR   Mueller-Dieckmann Jochen J  

Acta crystallographica. Section F, Structural biology and crystallization communications 20120731 Pt 8


LipS is a novel thermostable putative lipase that was isolated from a metagenomic library using functional screening methods. The corresponding gene shows high similarity to that encoding a putative but uncharacterized esterase from Symbiobacterium thermophilum IAM14863 (99% nucleotide-sequence similarity). Two different constructs of the recombinant lipase were crystallized. Crystals belonging to space group P4(2)2(1)2 diffracted X-ray radiation to 2.8 Å resolution and crystals belonging to spa  ...[more]

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