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Article

Calcium-independent opening of lid1 of a family I.3 lipase by a single Asp to Arg mutation at the calcium-binding site.

Protein engineering, design & selection : PEDS - 1 May 2014

Cheng M, Angkawidjaja C, Koga Y, Kanaya S

Abstract excerpt

A family I.3 lipase from Pseudomonas sp. MIS38 (PML) has two lids, lid1 and lid2, which are open when it exhibits activity. A single calcium ion is required to anchor lid1 in the open conformation by coordination with two acidic residues (Asp153 and Asp157) in lid1 and three other residues. Lid1 adopts a long α-helix in the open conformation, whereas it is sharply bent within this helix, such that Asp153 and...

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Source

Identifiers

PMID: 24737906
DOI: 10.1093/protein/gzu009

Genes

PML

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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