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The amino acid sequence of a type I copper protein with an unusual serine- and hydroxyproline-rich C-terminal domain isolated from cucumber peelings.
Max-Planck-Institut für Biochemie, Martinsried, Germany.
We have determined the amino acid sequence of a small copper protein isolated from cucumber peelings. This cupredoxin contains 137 amino acids including a pyroglutamate as the first residue. The N-terminal 110 amino acid-long domain shows 30-37% identity to 2 other cupredoxins, stellacyanin and cucumber basic blue protein. A unique feature of this protein is a 27 amino acid-long C-terminal domain rich in 4-hydroxyproline and serine and resembling certain plant cell wall proteins. The prolines in this domain are hydroxylated to a different extent depending on the surrounding sequence.
PMID: 1468551 [PubMed - indexed for MEDLINE]
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Cited by 4 PubMed Central articles
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Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of phytocyanins: plant-specific mononuclear blue copper proteins.
Nersissian AM, Immoos C, Hill MG, Hart PJ, Williams G, Herrmann RG, Valentine JS.
Protein Sci. 1998 Sep; 7(9):1915-29.
[Protein Sci. 1998]
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Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form.
Nersissian AM, Mehrabian ZB, Nalbandyan RM, Hart PJ, Fraczkiewicz G, Czernuszewicz RS, Bender CJ, Peisach J, Herrmann RG, Valentine JS.
Protein Sci. 1996 Nov; 5(11):2184-92.
[Protein Sci. 1996]
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ReviewThe structure and function of proline-rich regions in proteins.
Williamson MP.
Biochem J. 1994 Jan 15; 297 ( Pt 2):249-60.
[Biochem J. 1994]
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