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The Open Protein Structure Annotation Network
PDB Keyword
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3fez

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

    Title Crystal structure of uncharacterized ferredoxin fold protein related to antibiotic biosynthesis monooxygenases (YP_014836.1) from LISTERIA MONOCYTOGENES 4b F2365 at 2.10 A resolution. To be published
    Site JCSG
    PDB Id 3fez Target Id 390913
    Molecular Characteristics
    Source Listeria monocytogenes str. 4b f2365
    Alias Ids TPS20170,YP_014836.1, 3.30.70.900, 85268 Molecular Weight 19451.19 Da.
    Residues 167 Isoelectric Point 6.65
    Sequence mkkvfittgtehylrqlmanytggnvtllqnfsqsllyqestgeklfqegaeyrvlqssgslkgfgvvv feyihlrdeeipiflqmyqraslhfsetpglqstkltkamnmnkfliisfwdsevffhdwkktplskei tnimkknntqsgfshediyhypefshdak
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.10 Rfree 0.227
    Matthews' coefficent 3.75 Rfactor 0.203
    Waters 87 Solvent Content 67.20

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 3fez
    1. Structure of the signal transduction protein TRAP (target of RNAIII-activating protein)
    K Henrick, M Hirshberg - Acta Crystallographica Section F: Structural , 2012 - scripts.iucr.org
     

    Protein Summary

    Pfam note: On building, this very soon overlapped with ABM PF03992, for which there are other known structures

     

    Gene SPOA0323 from Listeria monocytogenes 4b f2365 encodes the YP_165150 protein composed of 2 domains, N-terminal domain (1-53) and C-terminal domain (54-162), belonging to the ABM family (PF03992).  This target is a sequence homolog to another JCSG target NP_471648.1 from LISTERIA INNOCUA. The search results from NCBI sequence alignment suggest that the C-terminal domain of YP_165150.1 carries a conserved domain belong to ABM superfamily from residue 65 to 167 other than hypothetic protein. Based on SSM alignment, the N-terminal domain of this target should be a structural homolog to histidine kinase (the F subunit of 1A0O).  The C-terminal domain of YP_165150.1 is a structural homolog to the C-terminal domain of 1LQ9, a monoxygenase protein. The interface interaction suggests that the biomolecule of YP_050331.1 be a monomer.

     

    MG14572B_1.png

    Figure 1. Protein YP_165150.1 consists of two domains: N-terminal domain (1-53) and C-teriminal domain (54-162). 

     

    MG14572B_n_1.png

     

    Figure 2. The N-terminal domain of protein YP_165150.1,  residue 1 ~ 53

     

    MG14572B_n_2.png

     

    Figure 3. Protein YP_750721.1  (blue) is structural homolog to the histide kinase (F subunit of 1A0O. grey), 1HWU(Orange) and 1FFG(Yellow).

     

    MG14572B_c_1.png

    Figure 4. The C-terminal domain of protein YP_750721.1  carries a conserved domain belonging to the ABM superfamily.

     

    MG14572B_c_2.png

     

    Figure 5.  Protein YP_750721.1  is a structural homolog to the C-terminal domain of 1LQ9, which a monoxygenase protein.

     

    TOPSAN Links For Related Targets.

    http://www.topsan.org/Proteins/JCSG/390900

     

     

    References,

    1.    Sciara, G.,  Kendrew, S.G.,  Miele, A.E.,  Marsh, N.G.,  Federici, L.,  Malatesta, F.,  Schimperna, G.,  Savino, C.,  Vallone, B.   (2003) The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis  EMBO J.   22: 205-215   (PDB: 1LQ9)
     
    2.    Gouet, P.,  Chinardet, N.,  Welch, M.,  Guillet, V.,  Cabantous, S.,  Birck, C.,  Mourey, L.,  Samama, J.P.  (2001) Further insights into the mechanism of function of the response regulator CheY from crystallographic studies of the CheY--CheA(124--257) complex.  Acta Crystallogr.,Sect.D  57: 44-51I (PDB: 1FFG).
     
    3.    Welch, M.,  Chinardet, N.,  Mourey, L.,  Birck, C.,  Samama, J.P.   (1998) Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY.  Nat.Struct.Biol.   5: 25-29   (PBD: 1A0O)
     
    4.    Machado Benelli, E.,  Buck, M.,  Polikarpov, I.,  Maltempi de Souza, E.,  Cruz, L.M.,  Pedrosa, F.O.   (2002) Herbaspirillum seropedicae signal transduction protein PII is structurally similar to the enteric GlnK.  Eur.J.Biochem.   269: 3296-3303   (PDB: 1HWU)
     
     

    Ligand Summary

    Reviews

    References

     

    No references found.

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