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The Open Protein Structure Annotation Network
PDB Keyword
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3g3s

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

    Title Crystal structure of GCN5-related N-acetyltransferase-like protein (ZP_00874857) (ZP_00874857.1) from Streptococcus suis 89/1591 at 1.80 A resolution. To be published
    Site JCSG
    PDB Id 3g3s Target Id 380027
    Molecular Characteristics
    Source Streptococcus suis 98hah33
    Alias Ids TPS24239,SSUI_28JUL04_CONTIG259_REVISED_GENE1367, 87073 Molecular Weight 28132.36 Da.
    Residues 248 Isoelectric Point 4.65
    Sequence maeqmrrvarlfgdwpetiiwtclegtmgdiyvddsqspqsalalygrqsffgflagqphrdllkiceg kniilvpqnqawsdlieevygdgvrfftryatkkdtefdlghlqklvddlpesfdmklidrnlyetclv eewsrdlvgnyidveqfldlglgcvilhkgqvvsgassyasysagieievdtredyrglglakacaaql ilacldrglypswdahtltslklaeklgyeldkayqayewr
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.80 Rfree 0.239
    Matthews' coefficent 2.47 Rfactor 0.203
    Waters 532 Solvent Content 50.22

    Ligand Information
    Ligands
    Metals

    Jmol

     

    Protein Summary

    I have built a family for this sequence, B9WSV7, and it overlaps with Acetyltransf_1 PF00583 and FR47 PF08445, both of which are in the Clan: Acetyltrans-like (CL0257), with many structures.

    FN12429A / encodes a protein with 248 residues from STREPTOCOCCUS SUIS 89-1591.  The NCBI sequence alignment can not suggest any conserved domain, but it predicates target FN12429A should be an acetyltranferase.  This target consists of two sub-domains.  The structure homolog search(SSM) shows that both of N-terminal domain and C-terminal domain belong to acetyltransferase. The overall of structure FN12429A is a structural homolog to Mycobacterium tuberculosis Mycothiol Synthase (PDB ID: 2C27). In the C-terminal of FN12429A, a conversed active groove is observed for substrate binding.  In FN12429A, the structural conserved Glu 185 and Tyr 236 should be the general acid and general base corresponding to Glu234 and Tyr 294 in 2C27, respectively.  A cacodylate anion crystallization buffer is observed in the conversed groove of FN12429A.  Although FN12429A is composed of two GNAT domains, the structure comparison reveals that the only C-terminals domain of FN12439A may have the activity. There is some domain movement between the N-terminal domains. Without further clues, the activity of N-terminal domain of FN12429A is still unclear.

     

    380027_1.png

     

     

    Figure 1. Protein FN12429A  consists of two domains, both of them belong to GNAT family.

     

     

    380027_2.png

     

    Figure 2. There are two subunits in each asymmetric unit. The  biomolecule of FN12429A should be a monomer, which has been approved by SEC/SLS results.

     

     

    380027_3.png

    Figure 3. Protein NP_639274.1 (green) is structural homolog to 2C27.

     

    380027_4.png

     

    Figure 4.  The active groove in 2C27 for substrate binding.

     

     

    380027_5.png

     

    Figure 5. The conserved groove in FN12429. Structurally conserved Glu 185

    and Tyr 234 are the general acid and base, respectively.

     

    Start of the paragraph contributed by Piotr Kozbial  --

    ZP_00874857 (GenBank) is a two domain protein with GCN5-related N-acetyltransferase-like C-terminal domain. Its conserved residues (see attached files) map to a cleft that is big enough to accommodate both a substrate and cofactor (acetyl-Coenzyme A or similar). Function of the N-terminal domain is unknown. The C-terminal domain is acetyltransferase-like, where residues 220-WDAHT-224 and Ser227 are likely to be close enough to currently unknown substrate and cofactor to include catalytic residues (if this protein has enzymatic activity). -- end of Piotr Kozbial contribution.

    References,

    1.    Vetting, M.W.,  Yu, M.,  Rendle, P.M.,  Blanchard, J.S.   (2006) The substrate-induced conformational change of Mycobacterium tuberculosis mycothiol synthase.  J.Biol.Chem.   281: 2795-2802  

     

     

    Ligand Summary

    Cacodylate

    Reviews

    References

     

    No references found.

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