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Structural analysis of the transcriptional regulator homolog protein from Pyrococcus horikoshii OT3

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Title: Structural analysis of the transcriptional regulator homolog protein from Pyrococcus horikoshii OT3
Authors: Okada, Ui Browse this author
Sakai, Naoki Browse this author
Yao, Min Browse this author →KAKEN DB
Watanabe, Nobuhisa Browse this author
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: 1084
End Page: 1086
Publisher DOI: 10.1002/prot.20913
PMID: 16506234
Abstract: PH1061 is a hypothetical protein of 100 residues (11.4 kDa) from the hyperthermophilic archaebacterium, Pyrococcus horikoshii OT31, and is conserved among many archaeal and bacterial organisms. Although the functions in these organisms are still unknown, a Pfam2 database search revealed that PH1061 has a helix-turn-helix (HTH) motif (“HTH_5 motif” in the Pfam database), and suggested that it is a DNA-binding protein, like members of the ArsR family3. ArsR is a transcriptional repressor of the arsenic resistance operon in Escherichia coli and other members of this family involve zinc-sensing transcriptional repressors, such as CzrA4 from Staphylococcus aureus and SmtB5 from Synechococcus pcc7942. The primary sequence similarities to PH1061 are 20%, 21%, and 6.6% with ArsR, CzrA, and SmtB, respectively. There are 10 proteins with the HTH_5 motif in P. horikoshii, but none of their functions are known. For structure-based functional analysis, the three-dimensional structure of PH1061 was determined at a resolution of 2.05 Å using the multi-wavelength anomalous diffraction (MAD) 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 有意

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