Proline cis-trans isomers in calbindin D9k observed by X-ray crystallography.
Proline cis-trans isomers in calbindin D9k observed by X-ray crystallography.
复制标题
通过 X 射线晶体学观察钙结合蛋白 D9k 中的脯氨酸顺反异构体。
DOI：
10.1016/0022-2836(92)90976-q
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发表时间：
1992
影响因子：
5.6
通讯作者：
S. Forsén
中科院分区：
文献类型：
--
作者：
L. Svensson;E. Thulin;S. Forsén
在重组牛钙结合蛋白D9 k的结构中，通过晶体学方法确定为1.6 μ m分辨率，观察到脯氨酸处于混合的、近似相等的分布的顺反构象。在钙结合蛋白D9 k至2.3 μ m分辨率的结构测定中或在任何其他晶体学测定的蛋白质结构中尚未报道这种异构体。顺式转异构化发生在Gly 42和Pro43之间的肽键上，这与钙结合蛋白D9 k溶液的二维1H核磁共振谱实验结果一致。替代的骨架伸展已被建模，并通过立体化学限制的最小二乘细化的片段Lys 41至Pro43。最终R值为0.188。结构扰动伴随着thecis-transomerization被发现是非常本地化。最大的位置差异是在残基Gly 42处观察到的，其中氧原子的替代位置相距3.6 nm。
In a structure of recombinant bovine calbindin D9k, determined crystallographically to 1.6 Å resolution, a proline in mixed, approximately equally populated,cisandtransconformation is observed. Isomers of this kind have not been reported in structure determinations of calbindin D9kto 2.3 Å resolution or in any other crystallographically determined protein structure. Thecis-transisomerization occurs at the peptide bond between Gly42 and Pro43, which is in agreement with results from two-dimensional1H nuclear magnetic resonance spectroscopy experiments on solutions of calbindin D9k. Alternative backbone stretches have been modeled and refined by stereochemical restrained least-squares refinement for the segment Lys41 to Pro43. The finalR-value was 0.188. The structural perturbations accompanying thecis-transisomerization are found to be very localized. The largest positional differences are observed at residue Gly42, in which the alternative positions of the oxygen atom are 3.6 Å apart.
DOI：
--
发表时间：
1981
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Fullmer,CS;Wasserman,RH
通讯作者：
Wasserman,RH
影响因子：
5.6
作者：
STEWART, DE;SARKAR, A;WAMPLER, JE
通讯作者：
WAMPLER, JE
DOI：
10.1073/pnas.86.7.2195
发表时间：
1989-04-01
影响因子：
11.1
作者：
CHAZIN, WJ;KORDEL, J;FORSEN, S
通讯作者：
FORSEN, S