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・ Streptanthus fenestratus
・ Streptanthus glandulosus
・ Streptanthus gracilis
・ Streptanthus hispidus
・ Streptanthus howellii
・ Streptanthus insignis
・ Streptanthus longisiliquus
・ Streptanthus morrisonii
・ Streptanthus niger
・ Streptanthus oliganthus
・ Streptanthus polygaloides
・ Streptanthus tortuosus
・ Streptanthus vernalis
・ Streptartemon
・ Streptartemon glaber
Streptavidin
・ Streptaxidae
・ Streptaxis
・ Streptaxoidea
・ Streptazolin
・ Streptoalloteichus
・ Streptobacillus
・ Streptobacillus moniliformis
・ Streptocarpus
・ Streptocarpus rexii
・ Streptocaulon
・ Streptocephalus
・ Streptocephalus dendrophorus
・ Streptocephalus dendyi
・ Streptocephalus gracilis


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Streptavidin : ウィキペディア英語版
Streptavidin

Streptavidin is a 52.8 kDa protein purified from the bacterium ''Streptomyces avidinii''. Streptavidin homo-tetramers have an extraordinarily high affinity for biotin (also known as vitamin B7 or vitamin H). With a dissociation constant (Kd) on the order of ≈10−14 mol/L, the binding of biotin to streptavidin is one of the strongest non-covalent interactions known in nature. Streptavidin is used extensively in molecular biology and bionanotechnology due to the streptavidin-biotin complex's resistance to organic solvents, denaturants (e.g. guanidinium chloride), detergents (e.g. SDS, Triton), proteolytic enzymes, and extremes of temperature and pH.
==Structure==

The crystal structure of streptavidin with biotin bound was reported by two groups in 1989. The structure was solved using multi wavelength anomalous diffraction by Hendrickson et al. at Columbia University and using multiple isomorphous replacement by Weber et al. 〔 〕 at E. I. DuPont Central Research and Development Department. As of February 2012, there are 135 structures deposited in the Protein Data Bank. See (this link ) for a complete list. The N and C termini of the 159 residue full-length protein are processed to give a shorter ‘core’ streptavidin, usually composed of residues 13 - 139; removal of the N and C termini is necessary for the high biotin-binding affinity. The secondary structure of a streptavidin monomer is composed of eight antiparallel β-strands, which fold to give an antiparallel beta barrel tertiary structure. A biotin binding-site is located at one end of each β-barrel. Four identical streptavidin monomers (i.e. four identical β-barrels) associate to give streptavidin’s tetrameric quaternary structure. The biotin binding-site in each barrel consists of residues from the interior of the barrel, together with a conserved Trp120 from neighbouring subunit. In this way, each subunit contributes to the binding site on the neighbouring subunit, and so the tetramer can also be considered a dimer of functional dimers.

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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