1CRL

INSIGHTS INTO INTERFACIAL ACTIVATION FROM AN 'OPEN' STRUCTURE OF CANDIDA RUGOSA LIPASE

Summary for 1CRL

• Entry DOI: 10.2210/pdb1crl/pdb
• Descriptor: LIPASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: hydrolase(carboxylic esterase)
• Biological source: Candida rugosa
• Total number of polymer chains: 1
• Total formula weight: 57779.47

Authors

Grochulski, P.,Cygler, M. (deposition date: 1993-03-02, release date: 1994-01-31, Last modification date: 2024-10-23)

Primary citation

Grochulski, P.,Li, Y.,Schrag, J.D.,Bouthillier, F.,Smith, P.,Harrison, D.,Rubin, B.,Cygler, M.
Insights into interfacial activation from an open structure of Candida rugosa lipase.
J.Biol.Chem., 268:12843-12847, 1993

PubMed Abstract: The structure of the Candida rugosa lipase determined at 2.06-A resolution reveals a conformation with a solvent-accessible active site. Comparison with the crystal structure of the homologous lipase from Geotrichum candidum, in which the active site is covered by surface loops and is inaccessible from the solvent, shows that the largest structural differences occur in the vicinity of the active site. Three loops in this region differ significantly in conformation, and the interfacial activation of these lipases is likely to be associated with conformational rearrangements of these loops. The "open" structure provides a new image of the substrate binding region and active site access, which is different from that inferred from the structure of the "closed" form of the G. candidum lipase.

PubMed: 8509417

Experimental method

X-RAY DIFFRACTION (2.06 Å)