PDBsum entry 1lpp

Hydrolase

PDB id: 1lpp

Contents

Protein chain

534 a.a.

Ligands

NAG-NAG

NAG

HDS ×2

Metals

_CA ×2

Waters ×296

References listed in PDB file

Key reference

• Title: Analogs of reaction intermediates identify a unique substrate binding site in candida rugosa lipase.
• Authors: P.Grochulski, F.Bouthillier, R.J.Kazlauskas, A.N.Serreqi, J.D.Schrag, E.Ziomek, M.Cygler.
• Ref.: Biochemistry, 1994, 33, 3494-3500. [DOI no: 10.1021/bi00178a005]
• PubMed id: 8142346

Abstract

The structures of Candida rugosa lipase-inhibitor complexes demonstrate that the scissile fatty acyl chain is bound in a narrow, hydrophobic tunnel which is unique among lipases studied to date. Modeling of triglyceride binding suggests that the bound lipid must adopt a "tuning fork" conformation. The complexes, analogs of tetrahedral intermediates of the acylation and deacylation steps of the reaction pathway, localize the components of the oxyanion hole and define the stereochemistry of ester hydrolysis. Comparison with other lipases suggests that the positioning of the scissile fatty acyl chain and ester bond and the stereochemistry of hydrolysis are the same in all lipases which share the alpha/beta-hydrolase fold.

Secondary reference #1

• Title: Two conformational states of candida rugosa lipase.
• Authors: P.Grochulski, Y.Li, J.D.Schrag, M.Cygler.
• Ref.: Protein Sci, 1994, 3, 82-91. [DOI no: 10.1002/pro.5560030111]
• PubMed id: 8142901

Secondary reference #2

• Title: A structural basis for the chiral preferences of lipases
• Authors: M.Cygler, P.Grochulski, R.J.Kazlauskas, J.D.Schrag, F.Bouthillier, B.Rubin, A.N.Serregi, A.K.Gupta.
• Ref.: j am chem soc, 1994, 116, 3180.

Secondary reference #3

• Title: Insights into interfacial activation from an open structure of candida rugosa lipase.
• Authors: P.Grochulski, Y.Li, J.D.Schrag, F.Bouthillier, P.Smith, D.Harrison, B.Rubin, M.Cygler.
• Ref.: J Biol Chem, 1993, 268, 12843-12847.
• PubMed id: 8509417