کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2048318 1074076 2012 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Crystal structure of cce_0566 from Cyanothece 51142, a protein associated with nitrogen fixation in the DUF269 family
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Crystal structure of cce_0566 from Cyanothece 51142, a protein associated with nitrogen fixation in the DUF269 family
چکیده انگلیسی

The crystal structure for cce_0566 (171 aa, 19.4 kDa), a DUF269 annotated protein from the diazotrophic cyanobacterium Cyanothece sp. ATCC 51142, was determined to 1.60 Å resolution. Cce_0566 is a homodimer with each molecule composed of eight α-helices folded on one side of a three strand anti-parallel β-sheet. Hydrophobic interactions between the side chains of largely conserved residues on the surface of each β-sheet hold the dimer together. The fold observed for cce_0566 may be unique to proteins in the DUF269 family, hence, the protein may also have a function unique to nitrogen fixation. A solvent accessible cleft containing conserved charged residues near the dimer interface could represent the active site or ligand-binding surface for the protein’s biological function.Structured summary of protein interactionsDUF269 and DUF269bind by x-ray crystallography (View interaction)


► First structural characterization of a protein from the DUF269 family.
► Dali search indicates protein fold is unique in current protein space.
► Homodimer with each unit containing 8 α-helices and 3-strand anti-parallel β-sheet.
► Hydrophobic interactions between intermolecular β-sheets hold dimer together.
► Cleft containing conserved charged residues at dimer interface is possible active site.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 586, Issue 4, 17 February 2012, Pages 350–355
نویسندگان
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