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VAT‐1 from Torpedo is a membranous homologue of zeta crystallin
Author(s) -
Linial Michael,
Levius Orit
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81140-u
Subject(s) - crystallin , zinc finger , homology (biology) , structural similarity , biochemistry , biology , torpedo , alcohol dehydrogenase , chemistry , amino acid , enzyme , gene , receptor , acetylcholine receptor , transcription factor
VAT‐1 is a major protein from Torpedo synaptic vesicles. A protein data‐base search revealed a striking homology to ξ crystallin from guinea pig lens. The overall amino‐acid identity is 27%, and 58% similarity is reached by including conserved substitutions. The highest similarity (60% to 85%) between the two proteins is observed in five discrete domains, which are also conserved in zinc‐dependent dehydrogenases, particularly in the alcohol dehydrogenase family. The cofactor‐binding domain of oxidoreductases is conserved in VAT‐1 and in ξ crystallin. VAT‐1 preferably binds NADPH in the presence of zinc. In contrast with its homologous proteins, VAT‐1 is an integral membrane protein of synaptic vesicles.