Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins.
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.
Cygler
M
M
Biotechnology Research Institute, National Research Council of Canada, Montréal, Québec.
Schrag
J D
JD
Sussman
J L
JL
Harel
M
M
Silman
I
I
Gentry
M K
MK
Doctor
B P
BP
D000595:Amino Acid Sequence; D000818:Animals; D004950:Esterases / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D008049:Lipase / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D011506:Proteins; D004950:Esterases; D008049:Lipase