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 Crystal structure of putative Lipoate-protein ligase (np_345629.1) from Streptococcus pneumoniae tigr4 at 1.99 A resolution. To be published
    Site JCSG
    PDB Id 1vqz Target Id 358040
    Molecular Characteristics
    Source Streptococcus pneumoniae tigr4
    Alias Ids TPS1382,NP_345629.1, 89889 Molecular Weight 37734.02 Da.
    Residues 329 Isoelectric Point 5.59
    Sequence mkyiinhsndtafnialeeyafkhlldedqifllwinkpsiivgrhqntieeinrdyvrengievvrri sgggavyhdlnnlnytiiskedenkafdfksfstpvintlaqlgvkaeftgrndleidgkkfcgnaqay ingrimhhgcllfdvdlsvlanalkvskdkfeskgvksvrarvtniinelpkkitvekfrdllleymkk eypemteyvfseeelaeinrikdtkfgtwdwnygkspefnvrrgikftsgkvevfanvteskiqdikiy gdffgiedvaavedvlrgvkyeredvlkalktiditryfagisreeiaeavvg
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.99 Rfree 0.21691
    Matthews' coefficent 2.19 Rfactor 0.15913
    Waters 285 Solvent Content 43.41

    Ligand Information


    Google Scholar output for 1vqz
    1. The Buccaneer software for automated model building. 1. Tracing protein chains
    K Cowtan - Acta Crystallographica Section D: Biological , 2006 - scripts.iucr.org
    2. 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
    3. Crystal Structure of Lipoate-Protein Ligase A Bound with the Activated Intermediate
    KH Kim, HH Lee, SJ Lee, JY Ha, HJ Yoon - Journal of Biological , 2005 - ASBMB
    4. Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution
    ZA Wood, LH Weaver, PH Brown, D Beckett - Journal of molecular , 2006 - Elsevier
    5. LplA1_dependent utilization of host lipoyl peptides enables Listeria cytosolic growth and virulence
    KM Keeney, JA Stuckey - Molecular , 2007 - Wiley Online Library
    6. Crystal structure of bovine lipoyltransferase in complex with lipoyl-AMP
    K Fujiwara, H Hosaka, M Matsuda - Journal of molecular , 2007 - Elsevier
    7. A unique lipoylation system in the Archaea
    MG Posner, A Upadhyay, S Bagby, DW Hough - Febs , 2009 - Wiley Online Library
    8. Lipoate-Protein Ligase A: Structure and Function
    K Fujiwara, H Hosaka, A Nakagawa - OXIDATIVE STRESS , 2008 - books.google.com

    Protein Summary

    The gene SP_1160 from Streptococcus pneumoniae encodes the NP_345629 protein, a putative lipoate-protein ligase A (LplA) EC: COG0095.  The N-terminal region (1-150) belongs to the lipoate protein ligase group (PF03099) and the C-terminus to the bacterial lipoate protein ligase C-terminus group (PF10437).

    SCOP classifies 1vqz N-terminal fragment (1-240) in the alpha+beta class, biotin synthetases superfamily, Lpl-like family; the C-terminal fragment (242-329) in the alpha+beta class, SufE/NifU superfamily, SP1160 C-terminal domain-like family. DALI top hits are with lipoate protein ligase A PDB:1x2h (Z=30), PDB:2c8m (Z=27), PDB:2art (Z=26), and the lipoyltransferase-1 PDB:3a7u (Z=25).

    LplA catalyzes the formation of lipoyl-AMP from lipoate and ATP and then transfers the lipoyl moiety to a specific lysine residue on the acyltransferase subunit of α-ketoacid dehydrogenase complexes and on H-protein of the glycine cleavage system.  It requires Mg2+ for catalysis.  Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, including pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) [Ref]. The amino acid sequence of this enzyme contains signature motif rrisgggavyhd, characteristic for this family.  Several structures of its E.coli homologues have been solved 1X2H 1X2G.  

    Ligand Summary





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