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The Open Protein Structure Annotation Network
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3lov

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

    Title Crystal structure of Putative protoporphyrinogen oxidase (YP_001813199.1) from Exiguobacterium sp. 255-15 at 2.06 A resolution. To be published
    Site JCSG
    PDB Id 3lov Target Id 396730
    Molecular Characteristics
    Source Exiguobacterium sibiricum 255-15
    Alias Ids TPS25448,YP_001813199.1, 332878 Molecular Weight 52425.73 Da.
    Residues 474 Isoelectric Point 4.87
    Sequence msskrlvivgggitglaaayyaerafpdlnitlleagerlggkvatyredgftiergpdsyvarkhilt dlieaiglgeklvrnntsqafildtgglhpipkgavmgiptdldlfrqttllteeekqevadlllhpsd slripeqdiplgeylrprlgdalvekliepllsgiyagnidqmstfatypqfvaneqkagslfegmrlm rpldqlpqtpqttikatgqflsletgleslierleevlerseirletpllaisredgryrlktdhgpey adyvlltiphpqvvqllpdahlpeleqltthstatvtmifdqqqslpiegtgfvvnrrapysitactai dqkwnhsapdhtvlrafvgrpgndhlvhesdevlqqavlqdlekicgrtlepkqviisrlmdglpaytv ghadriqrvreevlaqypgiylaglaydgvglpdcvasaktmiesieleqshtdesvnet
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.06 Rfree 0.241
    Matthews' coefficent 2.79 Rfactor 0.197
    Waters 308 Solvent Content 55.91

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 3lov
    1. Data processing and analysis with the autoPROC toolbox
    C Vonrhein, C Flensburg, P Keller, A Sharff - Section D: Biological , 2011 - scripts.iucr.org
     
    2. FAD-binding site and NAD (P) reactivity in human renalase, a new enzyme involved in blood pressure regulation
    M Milani, F Ciriello, S Baroni, V Pandini - Journal of Molecular , 2011 - Elsevier
     

    Protein Summary

    This protein is a protoporphyrinogen oxidase (PPO) based on high sequence similarity to B. subtilis enzyme 3i6d (40% id, Pubmed id: 19944166), which an important enzyme in the biosynthesis of heme/chlorophyll. It is also homologous to plant PPO (PDB 1sez, 21% seq, Pubmed  15057273).

     

    As expected, the structure is highly similar to the BsPPO. There is no ligand in the jcsg structure, except for co-factor FAD. The main value of this structure is that is an apo form, which displays a closed active site, suggesting conformational changes are needed for substrate binding.

     

    This protein is now in family PF01593.17 Amino_oxidase CL0063 along with other structures.

     

    Fig 1. PPO with FAD
    ge8204a.png

    Ligand Summary

    Reviews

    References

     

    No references found.

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    Files (1)

    FileSizeDateAttached by 
     ge8204a.png
    ge8204a monomer
    165.63 kB20:48, 1 Feb 2010qxuActions
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