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Relationship between sequence conservation and three‐dimensional structure in a large family of esterases, lipases, and related proteins
Author(s) -
Cygler Miroslaw,
Schrag Joseph D.,
Sussman Joel L.,
Harel Michal,
Silman Israel,
Gentry Mary K.,
Doctor Bhupendra P.
Publication year - 1993
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560020309
Subject(s) - torpedo , conserved sequence , lipase , protein secondary structure , peptide sequence , active site , biochemistry , protein structure , multiple sequence alignment , residue (chemistry) , stereochemistry , sequence alignment , chemistry , biology , enzyme , gene , receptor , acetylcholine receptor
Based on the recently determined X‐ray structures of Torpedo californica acetylcholinesterase and Geotrichum candidum lipase and on their three‐dimensional superposition, an improved alignment of a collection of 32 related amino acid sequences of other esterases, lipases, and related proteins was obtained. On the basis of this alignment, 24 residues are found to be invariant in 29 sequences of hydrolytic enzymes, and an additional 49 are well conserved. The conservation in the three remaining sequences is somewhat lower. The conserved residues include the active site, disulfide bridges, salt bridges, and residues in the core of the proteins. Most invariant residues are located at the edges of secondary structural elements. A clear structural basis for the preservation of many of these residues can be determined from comparison of the two X‐ray structures.