Structure of O67745_AQUAE, a hypothetical protein fromAquifex aeolicus
نویسندگان
چکیده
منابع مشابه
Crystal structure of conserved hypothetical protein Aq1575 from Aquifex aeolicus.
The crystal structure of a conserved hypothetical protein, Aq1575, from Aquifex aeolicus has been determined by using x-ray crystallography. The protein belongs to the domain of unknown function DUF28 in the Pfam and PALI databases for which there was no structural information available until now. A structural homology search with the DALI algorithm indicates that this protein has a new fold wi...
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Duanxiang Xu, Gaohua Liu, Rong Xiao, Tom Acton, Sharon Goldsmith-Fischman, Barry Honig, Gaetano T. Montelione, and Thomas Szyperski* Department of Chemistry, University at Buffalo, The State University of New York, Buffalo, New York Center of Advanced Biotechnology and Medicine and Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey Howard Hughes Medical...
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The gene product of structural genomics target Lmaj006129 from Leishmania major codes for a 164-residue protein of unknown function. When SeMet expression of the full-length gene product failed, several truncation variants were created with the aid of Ginzu, a domain-prediction method. 11 truncations were selected for expression, purification and crystallization based upon secondary-structure e...
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The genome of the bacterium Aquifex aeolicus encodes a polypeptide which is related to a small portion of a sequence found in one prokaryotic and two eukaryotic tRNA synthetases. It also is related to a portion of Arc1p, a tRNA-binding protein believed to be important for nuclear trafficking of tRNAs. Here we cloned, expressed and purified the 111 amino acid polypeptide (designated Trbp111) and...
متن کاملStructure and function of Rv0130, a conserved hypothetical protein from Mycobacterium tuberculosis.
A large fraction of the Mycobacterium tuberculosis genome codes for proteins of unknown function. We here report the structure of one of these proteins, Rv0130, solved to a resolution of 1.8 å. The Rv0130 monomer features a single hotdog fold composed of a highly curved beta-sheet on top of a long and a short alpha-helix. Two monomers in turn pack to form a double-hotdog-folded homodimer, simil...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section F Structural Biology and Crystallization Communications
سال: 2007
ISSN: 1744-3091
DOI: 10.1107/s1744309107018945