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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Atomic resolution structure of biotin-free Tyr43Phe streptavidin: what is in the binding site?
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Atomic resolution structure of biotin-free Tyr43Phe streptavidin: what is in the binding site?

机译：原子分辨率biotin-free结构Tyr43Phe链霉亲和素:什么是绑定网站吗?

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摘要

The streptavidin-biotin system is an example of a high-affinity protein-ligand pair (Ka approximately 10(13) mol-1). The thermodynamic and structural properties have been extensively studied as a model system for protein-ligand interactions. Here, the X-ray crystal structure of a streptavidin mutant of a residue hydrogen bonding to biotin [Tyr43Phe (Y43F)] is reported at atomic resolution (1.14 A). The biotin-free structure was refined with anisotropic displacement parameters (SHELXL97 program package). The high-resolution data also allowed interpretation of side-chain and residue disorder in 41 residues where alternate conformations were refined. The Y43F mutation is unambiguously observed in difference maps, although only a single O atom per monomer is altered. The atomic resolution enabled the identification of 2-methyl-2, 4-pentanediol (MPD) molecules in the biotin-binding pocket for the first time. Electron density for MPD was observed in all four subunit binding sites of the tetrameric protein. This was not possible with data at lower resolution (1.8-2.3 A) for wild-type streptavidin or mutants in the same crystal form using MPD in the crystallization. The impact of MPD binding on these studies is discussed.
机译：streptavidin-biotin系统的一个例子高亲和性protein-ligand一对(Ka大约10 (13)mol-1)。和结构都进行了广泛的属性研究了作为protein-ligand模型系统交互。链霉亲和素突变体的残余氢结合生物素(Tyr43Phe (Y43F)]在原子分辨率biotin-free(1.14)。结构改进与各向异性位移参数(SHELXL97程序包)。侧链的解释和残留障碍在41残留交替构象雅致。观察到在不同的地图,虽然只有一个单原子O /单体是改变。启用识别的决议2-methyl-2 4-pentanediol (MPD)分子首次biotin-binding口袋。MPD在所有四个电子密度四聚物的蛋白质的亚基结合位点。这是不可能的,数据较低分辨率为野生型链霉亲和素(1.8 - -2.3)或使用MPD在突变体在同一晶体形式的结晶。讨论了这些研究。

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