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1vjo

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

    Title Crystal structure of an alanine-glyoxylate aminotransferase from Anabaena sp. at 1.70 A resolution reveals a noncovalently linked PLP cofactor. Proteins 58 971-975 2005
    Site JCSG
    PDB Id 1vjo Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1319,17130350, 3.40.640.10
    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 2.06 Rfactor 0.15135
    Waters
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    Solvent Content 39.95

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1vjo
    1. The Buccaneer software for automated model building. 1. Tracing protein chains
    K Cowtan - Acta Crystallographica Section D: Biological , 2006 - scripts.iucr.org
     
    2. The importance of alignment accuracy for molecular replacement
    R Schwarzenbacher, A Godzik - Section D: Biological , 2004 - scripts.iucr.org
     
    3. Revisit of aminotransferase in the genomic era and its application to biocatalysis
    BY Hwang, BK Cho, H Yun, K Koteshwar - Journal of Molecular , 2005 - Elsevier
     
    4. On the combination of molecular replacement and single-wavelength anomalous diffraction phasing for automated structure determination
    S Panjikar, V Parthasarathy, VS Lamzin - Section D: Biological , 2009 - scripts.iucr.org
     
    5. Crystal structure of an alanine_glyoxylate aminotransferase from Anabaena sp. at 1.70 resolution reveals a noncovalently linked PLP cofactor
    G Won Han, R Schwarzenbacher - Proteins: Structure, , 2005 - Wiley Online Library
     
    6. An aminotransferase branch point connects purine catabolism to amino acid recycling
    I Ramazzina, R Costa, L Cendron, R Berni - Nature Chemical , 2010 - nature.com
     
    7. Theoretical study on 3-hydroxykynurenine transaminase by homology modeling and molecular dynamics
    QC Zheng, ZS Li, M Sun, Y Zhang, CC Sun - Polymer, 2005 - Elsevier
     
    8. Applications of Bioinformatics to Protein Structures: How Protein Structure and Bioinformatics Overlap
    GW Han, C Rife, MR Sawaya - Methods in Molecular Biology, 2009 - Springer
     
    9. PURIFICATION OF LYSINE DECARBOXYLASE: A MODEL SYSTEM FOR PLP ENZYME INHIBITOR DEVELOPMENT AND STUDY
    LC Zohner - 2011 - digitalcommons.unl.edu
     

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    Protein Summary

    Alanine-glyoxylate aminotransferase (AGT) from Anabaena sp. (EC 2.6.1.44; COG0075, Pfam00266) is a pyridoxal-phosphate (PLP) dependent enzyme involved in serine-glycine metabolism, where it catalyses the transamination of L-alanine and glyoxylate to pyruvate and glycine.

    The protein shows close structural resemblance with the human alanine:glyoxylate aminotransferase. In humans, where AGT is peroxisomal, a single point mutation miss-localizes the protein to the mitochondrion, leading to the hereditary kidney stone disease: primary hyperoxaluria type 1 (PubMed:12686111). AGT peroxisomal or mitochondrial location is species-dependent and related to diet in mammals (PubMed:14739251).

    Anabaena AGT forms dimer in crystal structure; where each monomer has fold of PLP-dependent transferases (SCOP sunid: 53382). The main N-terminal domain has 3 layers: ???, mixed ?-sheet of 7 strands, order 3245671; strand 7 is antiparallel to the rest. The C-terminal domain is a 2-layer ?? structure, with the 3-stranded, antiparallel ?-sheet packs against the edge of the N-terminal domain (PubMed:15657930).


    Ligand Summary



    References

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