HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Science >
Peer-reviewed Journal Articles, etc >

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

Files in This Item:
manuscript.pdf264.81 kBPDFView/Open
Please use this identifier to cite or link to this item:

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
Watanabe, Nobuhisa Browse this author
Tanaka, Isao Browse this author
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
Abstract: PH1061 is a hypothetical protein of 100 residues (11.4 kDa) from the 1 hyperthermophilic archaebacterium, Pyrococcus horikoshii OT3 , and is conserved among many archaeal and bacterial organisms. Although the functions in these 2 organisms are still unknown, a Pfam database search revealed that PH1061 has a helix-turn-helix (HTH) motif (“HTH_5 motif” in the Pfam database), and suggested that 3 it is a DNA-binding protein, like members of the ArsR family . ArsR is a transcriptional repressor of the arsenic resistance operon in Escherichia coli and other members of this 4 family involve zinc-sensing transcriptional repressors, such as CzrA from 5 Staphylococcus aureus and SmtB 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 A using the multi-wavelength anomalous diffraction (MAD) method.
Rights: Copyright (c) 2006 Wiley-Liss, Inc.
Relation URI:
Type: article (author version)
Appears in Collections:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 岡田 有意


Feedback - Hokkaido University