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Paquet, F ; Culard, F ; Barbault, F ; Maurizot, JC ; Lancelot, G

NMR solution structure of the archaebacterial chromosomal protein MC1 reveals a new protein fold

Biochemistry 43 (47) 14971-14978

par Administrateur - publié le

Abstract :

The three-dimensional structure of methanogen chromosomal protein 1 (MC 1), a chromosomal protein extracted from the archaebacterium Methanosarcina sp. CHT155, has been solved using H-1 NMR spectroscopy. The small basic protein MC1 contains 93 amino acids (24 basic residues against 12 acidic residues). The main elements of secondary structures are an a helix and five ß strands, arranged as two antiparallel ß sheets (a double one and a triple one) packed in an orthogonal manner forming a barrel. The protein displays a largely hydrophilic surface and a very compact hydrophobic core made up by side chains at the interface of the two ß sheets and the helix side facing the interior of the protein.