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PMID: 6442995 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Comparison of goose-type, chicken-type, and phage-type lysozymes illustrates the changes that occur in both amino acid sequence and three-dimensional structure during evolution.

Journal of molecular evolution ·Vol. 21 ·No. 2 ·1984-00-00 ·Pages 97-111

Weaver LH, Grütter MG, Remington SJ, Gray TM, Isaacs NW, Matthews BW

Abstract

The three-dimensional structure of goose-type lysozyme (GEWL), determined by x-ray crystallography and refined at high resolution, has similarities to the structures of hen (chicken) egg-white lysozyme (HEWL) and bacteriophage T4 lysozyme (T4L). The nature of the structural correspondence suggests that all three classes of lysozyme diverged from a common evolutionary precursor, even though their amino acid sequences appear to be unrelated (Grütter et al. 1983). In this paper we make detailed comparisons of goose-type, chicken-type, and phage-type lysozymes. The lysozymes have undergone conformational changes at both the global and the local level. As in the globins, there are corresponding alpha-helices that have rigid-body displacements relative to each other, but in some cases corresponding helices have increased or decreased in length, and in other cases there are helices in one structure that have no counterpart in another. Independent of the overall structural correspondence among the three lysozyme backbones is another, distinct correspondence between a set of three consecutive alpha-helices in GEWL and three consecutive alpha-helices in T4L. This structural correspondence could be due, in part, to a common energetically favorable contact between the first and the third helices. There are similarities in the active sites of the three lysozymes, but also one striking difference. Glu 73 (GEWL) spatially corresponds to Glu 35 (HEWL) and to Glu 11 (T4L). On the other hand, there are two aspartates in the GEWL active site, Asp 86 and Asp 97, neither of which corresponds exactly to Asp 52 (HEWL) or Asp 20 (T4L). (The discrepancy in the location of the carboxyl groups is about 10 A for Asp 86 and 4 A for Asp 97.) This lack of structural correspondence may reflect some differences in the mechanisms of action of the three lysozymes. When the amino acid sequences of the three lysozyme types are aligned according to their structural correspondence, there is still no apparent relationship between the sequences except for possible weak matching in the vicinity of the active sites.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Binding Sites Biological Evolution Birds/genetics Chickens/genetics Geese/genetics Models, Molecular Muramidase/genetics Protein Conformation Structure-Activity Relationship T-Phages/enzymology,genetics
Chemicals
Muramidase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Weaver L H
Grütter M G
Remington S J
Gray T M
Isaacs N W
Matthews B W
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Article Info
Journal
Journal of molecular evolution
Abbr.
J Mol Evol
ISSN
0022-2844
DOI
10.1007/BF02100084
Published
1984-00-00
Pages
97-111
Language
English
Region
Germany
NLM ID
0360051
Subset
IM
Grants
NIGMS NIH HHS · GM 20066 · United States
NIGMS NIH HHS · GM 21967 · United States
External Links
PubMed source DOI: 10.1007/BF02100084 View journal details
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