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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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