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The Open Protein Structure Annotation Network
PDB Keyword
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1vqz

    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
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1382,NP_345629.1, 89889
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

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

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    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
     

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    Protein Summary

    The gene SP_1160 from Streptococcus pneumoniae encodes the NP_345629 protein, a putative lipoate-protein ligase A (LplA) EC:2.7.7.63 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

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    (Z=30),
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    (Z=27),
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    (Z=26), and the lipoyltransferase-1
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    (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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