Protein and Gene Structure of a Chlorocruorin Chain of Eudistylia vancouverii
| Autor: | Marie-Louise Van Hauwaert, Andy Vierstraete, Serge N. Vinogradov, Luc Moens, Sylvia Dewilde, Jacques R. Vanfleteren |
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| Rok vydání: | 2001 |
| Předmět: |
Hemeproteins
DNA Complementary Chlorocruorin Annelida Molecular Sequence Data Biophysics Biochemistry chemistry.chemical_compound Eudistylia hemic and lymphatic diseases Animals Amino Acid Sequence Globin Molecular Biology Heme Chromatography High Pressure Liquid Phylogeny chemistry.chemical_classification Base Sequence Sequence Homology Amino Acid biology Intron DNA Sequence Analysis DNA Cell Biology biology.organism_classification Introns Globins Amino acid Globin fold chemistry Electrophoresis Polyacrylamide Gel Protein quaternary structure |
| Zdroj: | Biochemical and biophysical research communications |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.2001.4284 |
| Popis: | The polychaete annelid, Eudistylia vancouverii, contains as oxygen carrier a hexagonal bilayer (HBL) chlorocruorin. One of the globin chains, chain a1, has 142 amino acids (Mr 16,054.99) and its sequence deviates strongly from other nonvertebrate globin sequences. Unprecedented, it displays a Phe at the distal position E7 as well as at position B10, creating a very hydrophobic heme pocket probably responsible for the low oxygen affinity of the native molecule. Phylogenetic analysis of annelid globin chains clearly proves that globin chain a1 belongs to type I of globin chains having a pattern of 3 cysteine residues essential for the aggregation into a HBL structure. The gene coding for globin chain a1 is interrupted by 2 introns at the conserved positions B12.2 and G7.0. Based on protein and gene structure it can therefore be concluded that the globin chains of chlorocruorins are not fundamentally different from other annelid globin chains. |
| Databáze: | OpenAIRE |
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