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

    Title Crystal structure of N-acetylglucosamine kinase (EC (TM1224) from Thermotoga maritima at 2.46 A resolution. To be published
    Site JCSG
    PDB Id 2hoe Target Id 359804
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1437,TM1224, _0104.001898_, 429690 Molecular Weight 40884.93 Da.
    Residues 368 Isoelectric Point 5.57
    Sequence mpksvraenisrilkrimkspvsrvelaeelgltkttvgeiakiflekgivveekdspkgvgrptkslk ispncayvlgievtrdeiaaclidasmnilaheahplpsqsdreetlnvmyriidrakdmmeklgskls altvaapgpidtergiiidprnfplsqiplanllkekygievwvendadmgavgekwytkrddsfawil tgkgigagiiidgelyrgengyageigytrvfngneyvfledvcnenvvlkhvlsmgfsslaeardsgd vrvkeyfddiaryfsigllnlihlfgiskiviggffkelgenflkkikievethllykhsvdmsfskvq epviafgaavhalenylervtts
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.46 Rfree 0.271
    Matthews' coefficent 2.29 Rfactor 0.216
    Waters 15 Solvent Content 46.39

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    Ligand Information


    Google Scholar output for 2hoe
    1. Functional importance of Crenarchaea-specific extra-loop revealed by an X-ray structure of a heterotetrameric crenarchaeal splicing endonuclease
    S Yoshinari, T Shiba, DK Inaoka, T Itoh - Nucleic acids , 2009 - Oxford Univ Press
    2. A conserved lysine residue in the crenarchaea-specific loop is important for the crenarchaeal splicing endonuclease activity
    M Okuda, T Shiba, DK Inaoka, K Kita, G Kurisu - Journal of molecular , 2011 - Elsevier
    3. Structural Studies of ROK Fructokinase YdhR from Bacillus subtilis: Insights into Substrate Binding and Fructose Specificity
    B Nocek, AJ Stein, R Jedrzejczak, ME Cuff, H Li - Journal of Molecular , 2011 - Elsevier

    Protein Summary

    The TM1224 of T. maritima encodes a protein with helix-turn-helix subdomain (cd00090) followed by N-acetylglucosamine kinase (EC The TM1224 is a member of COG1940 (NagC, transcriptional regulator/sugar kinase). This protein was previously annotated as transcriptional regulator, XylR-related.

    Putative function of TM1224: N-acetylmannosamine repressor Not a Kinase:

    When compared to a human N-acetylmannosamine kinase containing ‘bound’ ADP (PDB 3EO3), the TM1224 structure does not exhibit conservation of the ADP-binding residues. Specifically, the conserved threonine residue (T417) of the ATP-binding motif that hydrogen bonds to the gamma phosphate of the ATP molecule in kinases is replaced by an aspartate residue in TM1224 (D85). The introduction of a negative charge at this position suggests that ATP binding is unlikely due to repulsion of negative charges between aspartate and the ATP's polyphosphate tail. However, TM1224 does have a typical DNA-binding domain within the N-terminal HTH-motif. Cumulatively, analysis of the structural data leads to the hypothesis that TM1224 is solely a repressor protein, rather than a dual function repressor / kinase. Sugar Specificity: Comparison of the human N-acetylmannosamine kinase structure (PDB 3EO3) to the structure of TM1224 indicates that N-acetylmannosamine (NAM) would be the preferred substrate, rather than N-acetylglucosamine (NAG). All NAM-binding site residues (N184, D185, E232, E248) are conserved between NAM kinase and TM1224 indicating that NAM may be the preferred substrate. Therefore, TM1224 likely binds NAM as a repressor molecule that regulates DNA binding rather than as a phosphate acceptor (in a kinase reaction).

    BioLEd Contributors: Joseph Breheny, Kanishk Jain, Jennifer Patterson, Jaewoong Jang, Paulinder Mann, Hung Pham, Karthik Shastri, Songserea Wood, Kathryne Wren, Cameron Mura, Carol Price, Linda Columbus.

    Funded by NSF DUE 1044858.

    Ligand Summary





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