The Open Protein Structure Annotation Network
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title On the use of DXMS to produce more crystallizable proteins: structures of the T. maritima proteins TM0160 and TM1171. Protein Sci. 13 3187-3199 2004
    Site JCSG
    PDB Id 1sj5 Target Id 358348
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1389,TM0160 Molecular Weight 16145.69 Da.
    Residues 145 Isoelectric Point 4.73
    Sequence mrkawvktlaldrvsntpvvilgiegtnrvlpiwigaceghalalamekmefprplthdlllsvlesle arvdkviihslkdntfyatlvirdltytdeedeeaalididsrpsdaiilavktgapifvsdnlvekhs ielevne
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.80 Rfree 0.27555
    Matthews' coefficent 2.26 Rfactor 0.21571
    Waters Solvent Content 45.55

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    Ligand Information


    Google Scholar output for 1sj5
    1. On the use of DXMS to produce more crystallizable proteins: structures of the T. maritima proteins TM0160 and TM1171
    G Spraggon, D Pantazatos, HE Klock, IA Wilson - Protein , 2004 - Wiley Online Library
    2. Structural and biochemical investigation of the role in proofreading of a _ hairpin loop found in the exonuclease domain of a replicative DNA polymerase of the B
    M Hogg, P Aller, W Konigsberg, SS Wallace - Journal of Biological , 2007 - ASBMB

    Protein Summary

    The gene TM0160 from Thermotoga maritima encodes the NP_227975 protein of unknown function DUF151 PF02577. Analysis of TM0160 genome vicinity finds a possible functional partner based on shared neigborhood (score 0.87) with a geranyltrans-transferase (TM0161).

    SCOP classifies 1sj5 in the alpha+beta class, TM0160 fold and family. DALI finds no significant hits (Z<3).

    A BLAST sequence alignment includes the C-terminal domain of the UvrB/UvrC protein from Polaribacter sp. 2FDC with an E-value=3e-38, 31% amino acid sequence identity  and 7% gaps.  UvrB is the central component in the prokaryotic nucleotide excision repair system.

    Additionally, DUF151 can be related structurally to the family of response regulators REC, like CheY protein ( 3F7N).  The response regulators act as phosphorylation-activated switches that affect a cellular response, usually by transcriptional regulation. Most of these proteins consist of two domains, an N-terminal response regulator receiver domain, and a variable C-terminal effector domain with DNA-binding activity.  Thus, temptatively DUF151 could be a C-terminal effector domain with DNA-binding activity of either DNA repair enzyme or a REC-like protein.


    1SJ5 is the N-terminal fragment of 1VJL structure.

    Ligand Summary





    No references found.

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