کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2053099 | 1074255 | 2005 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
1.2Â Ã
crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: 1.2Â Ã
crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold 1.2Â Ã
crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold](/preview/png/2053099.png)
چکیده انگلیسی
The recently described pneumococcal histidine triad protein family has been shown to be highly conserved within the pneumococcus. As part of our structural genomics effort on proteins from Streptococcus pneumoniae, we have expressed, crystallised and solved the structure of PhtA-166-220 at 1.2Â Ã
using remote SAD with zinc. The structure of PhtA-166-220 shows no similarity to any protein structure. The overall fold contains 3β-strands and a single short α-helix. The structure appears to contain a novel zinc binding motif. The remaining 4 histidine triad repeats from PhtA have been modelled based on the crystal structure of the PhtA histidine triad repeat 2. From this modelling work, we speculate that only three of the five histidine triad repeats contain the residues in the correct geometry to allow the binding of a zinc ion.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 579, Issue 24, 10 October 2005, Pages 5353-5360
Journal: FEBS Letters - Volume 579, Issue 24, 10 October 2005, Pages 5353-5360
نویسندگان
A. Riboldi-Tunnicliffe, N.W. Isaacs, T.J. Mitchell,