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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 354073
    Molecular Characteristics
    Source Nostoc sp. pcc 7120
    Alias Ids TPS1319,17130350, 3.40.640.10 Molecular Weight 41866.81 Da.
    Residues 381 Isoelectric Point 5.78
    Sequence maqiisindnqrlqleplevpsrlllgpgpsnahpsvlqamnvspvghldpaflalmdeiqsllryvwq tenpltiavsgtgtaameatianavepgdvvligvagyfgnrlvdmagrygadvrtiskpwgevfslee lrtalethrpailalvhaetstgarqplegvgelcrefgtlllvdtvtslggvpifldawgvdlayscs qkglgcspgaspftmssraieklqrrrtkvanwyldmnllgkywgservyhhtapinlyyalrealrli aqeglancwqrhqknveylwerlediglslhvekeyrlptlttvcipdgvdgkavarrllnehnievgg glgelagkvwrvglmgfnsrkesvdqlipaleqvlr
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.70 Rfree 0.20182
    Matthews' coefficent 2.06 Rfactor 0.15135
    Waters 432 Solvent Content 39.95

    Ligand Information
    Ligands
    Metals

    Jmol

     
    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
     

    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

    Reviews

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