کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2048156 1074067 2011 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Novel structure of an N-terminal domain that is crucial for the dimeric assembly and DNA-binding of an archaeal DNA polymerase D large subunit from Pyrococcus horikoshii
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Novel structure of an N-terminal domain that is crucial for the dimeric assembly and DNA-binding of an archaeal DNA polymerase D large subunit from Pyrococcus horikoshii
چکیده انگلیسی

Archaea-specific D-family DNA polymerase forms a heterotetramer consisting of two large polymerase subunits and two small exonuclease subunits. The N-terminal (1–300) domain structure of the large subunit was determined by X-ray crystallography, although ∼50 N-terminal residues were disordered. The determined structure consists of nine alpha helices and three beta strands. We also identified the DNA-binding ability of the domain by SPR measurement. The N-terminal (1–100) region plays crucial roles in the folding of the large subunit dimer by connecting the ∼50 N-terminal residues with their own catalytic region (792–1163).Structured summaryDP2binds to DP2 by molecular sieving(View interaction)DP2binds to DP2 by fluorescence technology(View interaction)DP2binds to DP2 by circular dichroism(View interaction)

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 585, Issue 3, 4 February 2011, Pages 452–458
نویسندگان
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