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The Open Protein Structure Annotation Network
PDB Keyword
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References
    Title Comparison of NMR and crystal structures for the proteins TM1112 and TM1367. Acta Crystallogr.,Sect.F 66 1381-1392 2010
    Site JCSG
    PDB Id 2k9z Target Id 282978
    Related PDB Ids 1o5u 
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1262,TM1112 Molecular Weight 10756.93 Da.
    Residues 89 Isoelectric Point 5.50
    Sequence mevkiekptpeklkelsvekwpiwekevsefdwyydtnetcyilegkvevttedgkkyviekgdlvtfp kglrcrwkvlepvrkhynlf
      BLAST   FFAS

    Structure Determination
    Method NMR Chains 1

    Ligand Information
    Ligands
    Metals

    Jmol

     

    Protein Summary

    The TM1112 gene of Thermotoga maritima encodes the conserved hypothetical protein NP_228918 (Pfam05899; DUF861) with unknown function [Ref]. This family consists of several bacterial and plant proteins. TM1112 has similar phylogenetic cooccurrence (string.embl.de) as TM1189 (putative KAP NTPase), indicating that functions of both proteins may be interdependent.

    The 1o5u structure has a double-stranded beta-helix fold (SCOP sunid:51181), where one turn of helix is made by two pairs of antiparallel strands linked with short turns that has appearance of a sandwich of distinct architecture and jelly-roll topology. 1o5u belongs to the superfamily of RmlC-like cupins (SCOP sunid:51182), and has its own family. DALI top hits are with the DUF1255 protein 3eo6 (Z=11) and the uncharacterized protein 3bcw (Z=10).

    1o5u has a large number of similar (Z<8) structures (PDB:2b8m, PDB:1yhf, PDB:1vj2, PDB:1vr3, PDB:2f4p, PDB:2fqp, PDB:2atf, PDB:1v70, PDB:1zz6, PDB:1m4o, PDB:1xja, PDB:1qwr, PDB:1lr5, PDB:1yfu, PDB:1od5, PDB:1j3p, PDB:1sef, PDB:1y9q, PDB:1ey2, PDB:1sq4, PDB:1zvf, PDB:1uik, PDB:1o4t, PDB:1sfn, PDB:1rc6, PDB:1zx5, PDB:1vrb, PDB:1j58, PDB:2gm6, PDB:1tq5, PDB:2h0v, PDB:1ipj, PDB:2cv6, PDB:1fi2, PDB:2cau, PDB:1fxz, PDB:1x7n). However it is unknown what functional implications, if any, can be obtained on the basis of structural similarity to those structures.

    Analysis of the crystallographic packing of 1o5u using the PQS server {Henrick, 1998 #73} indicates that a monomer is the biologically relevant form. The alpha-helix 1 and 2 of 1o5u prevent dimerization of this protein in a way commonly observed for other proteins with cupin fold.

    Ligand Summary

    One of the unknown ligands (UNL401) interacts with residues from chain A: Tyr35, Glu39, Cys41, Trp76. This ligand is covalently bound to Lys84 from chain A.
    The UNL401 is located in a cleft containing highly conserved Trp24, Glu39, and Tyr86.


    References

    Reviews

    References

     

    1. McMullan D, Schwarzenbacher R, Jaroszewski L, von Delft F, Klock HE, Vincent J, Quijano K, Abdubek P, Ambing E, Biorac T, Brinen LS, Canaves JM, Dai X, Deacon AM, DiDonato M, Elsliger MA, Eshaghi S, Floyd R, Godzik A, Grittini C, Grzechnik SK, Hampton E, Karlak C, Koesema E, Kreusch A, Kuhn P, Levin I, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Page R, Reyes R, Rezezadeh F, Robb A, Sims E, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Wang X, West B, Wolf G, Xu Q, Hodgson KO, Wooley J, Lesley SA, and Wilson IA Crystal structure of a novel Thermotoga maritima enzyme (TM1112) from the cupin family at 1.83 A resolution. Proteins. 2004 Aug 15; 56(3):615-8 PubMed HubMed doi:10.1002/prot.20139 pmid:15229894.

       


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