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T. maritima Browser

TOPSAN > Proteins > JCSG > 2p1a

2p1a

    Page last modified 20:33, 24 Sep 2010 by Admin
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References
    Title Crystal structure of hypothetical protein (NP_978475.1) from Bacillus cereus ATCC 10987 at 2.10 A resolution. To be published
    Site JCSG
    PDB Id 2p1a Target Id 366831
    Molecular Characteristics
    Source Bacillus cereus atcc 10987
    Alias Ids TPS1478,NP_978475.1 Molecular Weight 17951.87 Da.
    Residues 153 Isoelectric Point 5.95
    Sequence mfvqsalhqlkvavdtsiqmldqyteidlkiapiqskrslfemyahlslichadllilngstekelhtf ykeqtpetiaqmqktmiqgydllsktflsysneqlaemktaywgisysrfewlleivahfyhhrgqihi llcehmkdpniplfq
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.10 Rfree 0.268
    Matthews' coefficent 2.10 Rfactor 0.221
    Waters 98 Solvent Content 41.35

    Ligand Information
    Ligands
    Metals

    Jmol

     

    Protein Summary

    The gene BCE_2162 from Bacillus cereus atcc 10987 encodes the NP_978475 amino acid sequence that belongs to the DinB superfamily (PF05163).

    SCOP classifies 2p1a in the all alpha class, DinB/YfiT-like putative metalloenzymes superfamily.

    Dali top hits for 2p1a are with 2hkv (Z-scr=18) and the YfiT-like protein 1rxq [Ref] (Z-scr=14).

    2p1a contains the characteristic triad of histidines that usually coordinate a nickel ion.  In particular the two histidines that are part of the C-terminal alpha helix contain the HXYHHR sequence motif that is also found in the 2hkv structure. So these two structures may share a common function.


     

    Ligand Summary



    References

    Reviews References Images Files Tags

    Reviews

    References

     

    1. Rajan SS, Yang X, Shuvalova L, Collart F, and Anderson WF YfiT from Bacillus subtilis is a probable metal-dependent hydrolase with an unusual four-helix bundle topology. Biochemistry. 2004 Dec 14; 43(49):15472-9 PubMed HubMed doi:10.1021/bi048665r pmid:15581359.

       


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