文章基本信息

标题：Crystal structure of conserved hypothetical protein Aq1575 from Aquifex aeolicus
本地全文：下载
作者：Dong Hae Shin ; Hisao Yokota ; Rosalind Kim 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2002
卷号：99
期号：12
页码：7980-7985
DOI：10.1073/pnas.132241399
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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 with no obvious similarity to those of other proteins of known three-dimensional structure. The protein reveals a monomer consisting of three domains arranged along a pseudo threefold symmetry axis. There is a large cleft with approximate dimensions of 10 A x 10 A x 20 A in the center of the three domains along the symmetry axis. Two possible active sites are suggested based on the structure and multiple sequence alignment. There are several highly conserved residues in these putative active sites. The structure based molecular properties and thermostability of the protein are discussed.
关键词：structural genomics|new fold|DUF28|hyperthermophile| thermostability