THE WAC GENE-PRODUCT OF BACTERIOPHAGE-T4 CONTAINS COILED-COIL STRUCTURAL PATTERNS

被引:15
作者
SOBOLEV, BN [1 ]
MESYANZHINOV, VV [1 ]
机构
[1] DI IVANOVSKII VIROL INST,DEPT BASIC VIROL,16 GAMALEYA ST,MOSCOW 123098,USSR
基金
美国国家科学基金会;
关键词
D O I
10.1080/07391102.1991.10507859
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The bacteriophage T4 late gene wac (whisker antigen control) encodes the protein which forms the fibrous structure on the neck of the virion called whiskers. Amino acid sequence analysis of wac gene product, as deduced from the nucleotide sequence, indicates ten alpha-helical domains (19-40 residues long) with coiled-coil structural patterns. These regions comprise about 70% of the entire 486 amino acid sequence. The alpha-helices are separated by short stretches of polypeptide chain which are similar to the loop regions of the globular protein sequences. We propose a structural model for the dimer of wac gene product molecule, that we call fibritin in which two polypeptide chains associate in a parallel fashion and form a segmented alpha-helical coiled-coil rod similar to epidermal keratins.
引用
收藏
页码:953 / 965
页数:13
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