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1zx8

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

    Title Crystal structure of TM1367 from Thermotoga maritima at 1.90 A resolution reveals an atypical member of the cyclophilin (peptidylprolyl isomerase) fold. Proteins 63 1112-1118 2006
    Site JCSG
    PDB Id 1zx8 Target Id 283228
    Related PDB Ids 2ka0 
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1280,TM1367, 289463, 90122 Molecular Weight 13922.43 Da.
    Residues 124 Isoelectric Point 4.86
    Sequence mrvellfesgkcvidlneeyevvkllkekipfesvvntwgeeiyfstpvnvqkmenprevveigdvgyw ppgkalclffgktpmsddkiqpasavnvigkivegledlkkikdgekvavrfass
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 3
    Resolution (Å) 1.90 Rfree 0.21
    Matthews' coefficent 2.31 Rfactor 0.166
    Waters 243 Solvent Content 46.39

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    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1zx8
    1. Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard
    TC Terwilliger, PD Adams, RJ Read - Section D: Biological , 2009 - scripts.iucr.org
     
    2. Crystal structure of TM1367 from Thermotoga maritima at 1.90 resolution reveals an atypical member of the cyclophilin (peptidylprolyl isomerase) fold
    KK Jin, S Krishna, R Schwarzenbacher - Proteins: Structure, , 2006 - Wiley Online Library
     
    3. Comparison of NMR and crystal structures for the proteins TM1112 and TM1367
    B Mohanty, P Serrano, B Pedrini - Section F: Structural , 2010 - scripts.iucr.org
     
    4. Insights into immunophilin structure and function
    C Lucke, M Weiwad - Current medicinal chemistry, 2011 - ingentaconnect.com
     
    5. Hypothetical protein AF2241 from Archaeoglobus fulgidus adopts a cyclophilin-like fold
    X Ai, L Li, A Semesi, A Yee, CH Arrowsmith - Journal of biomolecular , 2007 - Springer
     

    Protein Summary

    Gene TM1367 from Thermotoga maritima encodes the NP_229168 protein that belongs to the DUF369 (PF04126) family. Its structure (2ka0) reveals an atypical cyclophilin (peptidylprolyl cis-trans isomerase) fold [Ref]. Homologous sequences to TM1367 are found in bacteria and archaea only. TM1367 has sequence similar to proteins from COG2164 (Uncharacterized conserved protein) , COG4925 (Uncharacterized conserved protein), and COG4070 (predicted peptidyl-prolyl cis-trans isomerase (rotamase), cyclophilin family). 

    2ka0 belongs to the SCOP cyclophilin-like superfamily, TM1367-like family. 2ka0 (or its crystal structure PDB:1zx8) Dali hits are with PDB:2nnz (Z-scr=16), PDB:3kop (Z-scr=14), and cyclophilin B PDB:1j2a (Z-scr=11). Several conserved residues are part of putative ligand binding cleft (Trp39, Glu42, Tyr44, Trp69, Cys76, Phe78, Pro91, and Val95. In the structural alignment, residues Cys76 and Glu42 are not superimposed in the similar protein structures (i.e.: PDB structures: 2cpl and 1x7f).

    Ligand Summary



    References

    Reviews

    References

     

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