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Crystal structure of an RtcB homolog protein (PH1602-extein protein) fromPyrococcus horikoshii reveals a novel fold

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Title: Crystal structure of an RtcB homolog protein (PH1602-extein protein) fromPyrococcus horikoshii reveals a novel fold
Authors: Okada, Chiaki Browse this author
Maegawa, Yuki Browse this author
Yao, Min Browse this author →KAKEN DB
Tanaka, Isao Browse this author →KAKEN DB
Issue Date: Jun-2006
Publisher: Wiley-Liss
Journal Title: Proteins: Structure Function and Bioinformatics
Volume: 63
Issue: 4
Start Page: 1119
End Page: 1122
Publisher DOI: 10.1002/prot.20912
PMID: 16485279
Abstract: The hypothetical extein, PH1602-extein (53.5 kDa, 481 residues) from the hyperthermophilic archaebacterium, Pyrococcus horikoshii OT3, shows sequence similarity to Escherichia coli RtcB (33% identity). RtcB homologs are conserved in all archaebacteria, in most eukaryotes, including metazoa, and in a wide variety of eubacteria. In E. coli, the rtcB gene, together with rtcA and rtcR, comprise the 54-dependent operon termed the RNA 3-terminal phosphate cyclase operon. The functions of the gene products RtcA and RtcR have been characterized previously as RNA 3-terminal phosphate cyclase and 54-specific regulator, respectively. On the other hand, although RtcB is highly conserved among many organisms, there have been few studies of RtcB and its homologs. In a previous study, it was suggested that human RtcB homolog may form a heterotrimer with DDX1 (putative RNA helicase) and CGI-99 (ninein-interaction protein). These three proteins were pulled down by double-stranded DNA fragments. The artificial DNA sequences included an 11-bp inverted repeat, thus enabling formation of a cruciform structure. The manner of interaction between the presumptive trimer and double-stranded DNA has not been clarified. Sequence analysis indicated that the ph1602 gene encodes an RtcB homolog with an intervening intein. Thus, translation products of ph1602 are considered to generate two mature proteins, PH1602-intein and PH1602-extein, because of the protein-splicing activity of the intein. We cloned the extein sequence of PH1602 and successfully overexpressed, purified, and crystallized the PH1602-extein. Here, we report the crystal structure of PH1602-extein at 2.15 Å resolution, determined by the single-wavelength anomalous diffraction (SAD) method.
Rights: Copyright (c) 2006 Wiley-Liss, Inc.
Type: article (author version)
Appears in Collections:理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 岡田 知晃

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