The Open Protein Structure Annotation Network
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary

    Title Crystal structure of putative acetyltransferase (YP_390128.1) from Desulfovibrio desulfuricans G20 at 2.28 A resolution. To be published
    Site JCSG
    PDB Id 3c8v Target Id 377310
    Molecular Characteristics
    Source Desulfovibrio desulfuricans g20
    Alias Ids TPS1686,YP_390128.1, 104255 Molecular Weight 52867.88 Da.
    Residues 477 Isoelectric Point 5.85
    Sequence mtqlellleriidrvnvnlrhqkfdvgdyvrrqtphlhyskfyafyglsaddpvhfhfknsslagsyll grvnvlhsalyksdirgdelkrkgqhfvcdgkmiplhddevitikdsflnktlvhsnshdpespeefti rntvampyanihgsltegsfigsfatvdlstihnsvvryfsyvqtgelvgkcvepgqiwiksgdelefh ysfdkaildkyisqeagscptgvlmefvevrqedfeevfasghmasgagsasgasvsgyavikgdtvig envlvsqrayldnawmgkgsnaqencyiinsrlerncvtahggkiinahlgdmiftgfnsflqgsessp lkigdgcvvmphtiidleepleipaghlvwgyirnkadlaahsisfeefakvdgevtmgrmtfrgkggp fldsfkkrikrilsengaffdgsegtghaqkgknftfniiqpyqdgdprgmyptiliqpnngs
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 4
    Resolution (Å) 2.28 Rfree 0.223
    Matthews' coefficent 2.82 Rfactor 0.180
    Waters 540 Solvent Content 56.34

    Ligand Information


    Google Scholar output for 3c8v
    1. The three-dimensional Structure of a mycobacterial DapD provides insights into DapD diversity and reveals unexpected particulars about the enzymatic mechanism
    L Schuldt, S Weyand, G Kefala, MS Weiss - Journal of molecular biology, 2009 - Elsevier

    Protein Summary

    This protein contains two domains of similar fold (1-210+447-477, 251-446) linked by a helix containing a beta hairpin (213-446). Each domain adopts typical UDP N-acetylglucosamine acyltransferase like fold. This organization of acyltransferase domains is novel.

    The sequence analysis using BLAST suggests that this protein contains a PaaY carbonic anhydrases acetyltransferase region (251-376). This region maps to the second domain of this protein. However, this domain lacks features such as insertions outside the triangle barrel. The first domain seems more feature-rich, and is structurally similar to part of N-acetylglucosamine-1-phosphate uridyltransferase (e.g. 1g97).

    This protein is likely to dimerize through its C-terminal 447-477 region. There are only 4 full length homologous sequences, all of them are highly homologous to each other.

    KEGG annotation of this protein seems to suggest that this protein is likely to involved in aminosugar metabolism and is likely multi-functional: UDP-N-acetylglucosamine pyrophosphorylase and glucosamine-1-phosphate N-acetyltransferase. The domain organization seems to support that.

    In summary, it seems that this protein catalyzes the following reactions:

    acyl transfer (in domain 2?):
    alpha-D-Glucosamine 1-phosphate ->N-Acetyl-D-glucosamine 1-phosphate
    uridyltransferase (domain 1?):
    N-Acetyl-D-glucosamine 1-phosphate <-> UDP-N-acetyl-D-glucosamine

    Further crystallographic characterization with above substrates should be fruitful.

    Ligand Summary




    No references found.

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