MOLECULAR SUBSTRUCTURE OF A VIRAL RECEPTOR-RECOGNITION PROTEIN - THE GP17 TAIL-FIBER OF BACTERIOPHAGE-T7
MOLECULAR SUBSTRUCTURE OF A VIRAL RECEPTOR-RECOGNITION PROTEIN - THE GP17 TAIL-FIBER OF BACTERIOPHAGE-T7
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DOI:
10.1016/0022-2836(88)90246-x
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发表时间:
1988-03-20
影响因子:
5.6
通讯作者:
STUDIER, FW
中科院分区:
文献类型:
--
作者:
STEVEN, AC;TRUS, BL;STUDIER, FW
The bacteriophage T7 tail complex consists of a conical tail-tube surrounded by six kinked tail-fibers, which are oligomers of the viral protein gp17 (Mr 61,400). We have derived a molecular model for the tail-fiber by integrating secondary structure predictions with ultrastructural information obtained by correlation averaging of electron micrographs of negatively stained tail complexes. This model has been further refined by high-resolution scanning transmission electron microscopy of purified fibers, both negatively stained and unstained. Mass measurements made from the latter images establish that the fiber is a trimer of gp17. The proximal half-fiber is a uniform rod, about 2.0 nm in diameter and 16.4 nm long, which we refer to be a triple-stranded coiled-coil, containing three copies of an .alpha.-helical domain of about 117 residues, starting at Phe151. The distal half-fiber is 15.5 nm long, and is made up of four globules, 3.1 to 4.8 nm in diameter, in rigid linear array: it contains the carboxy-terminal halves (residues .apprx. 268 to 553) of the constituent gp17 chains, arranged with 3-fold symmetry around its long axis. The amino-terminal domains (residues 1 to 149) link the fiber to the tail-tube. We conclude that the three gp17 chains are quasi-equivalent in the proximal half-fiber, equivalent in the distal half-fiber, and non-equivalent in the kink region that separates the two half-fibers: such localized non-equivalence may represent a general mechanism for the formation of kinked joints in segmented homo-oligomeric proteins.