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1j5y

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary

    Title Crystal structure of a transcription regulator (TM1602) from Thermotoga maritima at 2.3 A resolution. Proteins 67 247-252 2007
    Site JCSG
    PDB Id 1j5y Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1303,TM1602, RER070207001382, 84693
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 1
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 3.20 Rfactor 0.19
    Waters
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    Solvent Content 61.25

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1j5y
    1. Fido, a novel AMPylation domain common to fic, doc, and AvrB
    LN Kinch, ML Yarbrough, K Orth, NV Grishin - PLoS One, 2009 - dx.plos.org
     
    2. CASP5 target classification
    LN Kinch, Y Qi, TJP Hubbard - : Structure, Function, and , 2003 - Wiley Online Library
     
    3. Prediction of active sites for protein structures from computed chemical properties
    J Ko, LF Murga, Y Wei, MJ Ondrechen - Bioinformatics, 2005 - Oxford Univ Press
     
    4. Transcriptional regulation of NAD metabolism in bacteria: genomic reconstruction of NiaR (YrxA) regulon
    DA Rodionov, X Li, IA Rodionova, C Yang - Nucleic acids , 2008 - Oxford Univ Press
     
    5. Computational study of the heterodimerization between _ and _ receptors
    X Liu, M Kai, L Jin, R Wang - Journal of computer-aided molecular design, 2009 - Springer
     
    6. A fold-recognition approach to loop modeling
    C Levefelt, D Lundh - Journal of molecular modeling, 2006 - Springer
     
    7. Crystal structure of a transcription regulator (TM1602) from Thermotoga maritima at 2.3 resolution
    D Weekes, MD Miller, S Krishna - Proteins: Structure, , 2007 - Wiley Online Library
     
    8. Of sequence and structure: Strategies of protein thermostability in evolutionary perspective
    IN Berezovsky, EI Shakhnovich - Arxiv preprint q-bio/0408007, 2004 - arxiv.org
     

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    Protein Summary

    This protein is proposed to contain a 3-histidine (3H) domain, named after its three highly conserved histidines, and a DNA-binding domain. It represents the first structure of a 3H protein family member. Based on sequence analysis, its function has been postulated to involve binding of small molecules. Recent experimental data support this prediction, suggesting that it belongs to a family of de novo NAD synthesis pathway regulators that may bind to nicotinamide, nicotinic acid, or other substrate/products. When activated by these small molecules, it is proposed to bind to the NAD promoter region to repress the de novo NAD biosynthesis operon. This pathway has been well characterized in the TM1602 homologous protein, yrxA, from Bacillus subtilis. Experimental characterization of this protein is now in progress [Rodionov & Osterman].[Ref]

    Ligand Summary

    Reviews

    References

     

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