.
The Open Protein Structure Annotation Network
PDB Keyword
.

1o4u

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

    Title Crystal structure of a type II quinolic acid phosphoribosyltransferase (TM1645) from Thermotoga maritima at 2.50 A resolution. Proteins 55 768-771 2004
    Site JCSG
    PDB Id 1o4u Target Id 283502
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1308,TM1645, 85077 Molecular Weight 30179.27 Da.
    Residues 273 Isoelectric Point 5.08
    Sequence mekildllmsfvkedegkldlasfplrnttagahlllktenvvasgievsrmflekmgllskfnvedge ylegtgvigeiegntykllvaertllnvlsvmfsvatttrrfaeklkhakiaatrkilpglgvlqkiav vhgggdphrldlsgcvmikdnhlkmygsaeravqevrkiipfttkievevenledalraveagadivml dnlspeevkdisrrikdinpnvivevsggiteenvslydfetvdvisssrltlqevfvdlsleiqr
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.50 Rfree 0.27225
    Matthews' coefficent 3.57 Rfactor 0.21295
    Waters 113 Solvent Content 65.25

    Access denied for user 'root'@'localhost' (using password: YES) (click for details)

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1o4u
    1. The importance of alignment accuracy for molecular replacement
    R Schwarzenbacher, A Godzik - Section D: Biological , 2004 - scripts.iucr.org
     
    2. FRankenstein becomes a cyborg: the automatic recombination and realignment of fold recognition models in CASP6
    J Kosinski, MJ Gajda, IA Cymerman - PROTEINS: , 2005 - Wiley Online Library
     
    3. Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species
    SB Conners, EF Mongodin, MR Johnson - FEMS microbiology , 2006 - Wiley Online Library
     
    4. An iterative knowledge_based scoring function for proteinprotein recognition
    SY Huang, X Zou - Proteins: Structure, Function, and , 2008 - Wiley Online Library
     
    5. Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum
    DH Shin, N Oganesyan, J Jancarik, H Yokota - Journal of Biological , 2005 - ASBMB
     
    6. The JCSG MR pipeline: optimized alignments, multiple models and parallel searches
    R Schwarzenbacher, A Godzik - Section D: Biological , 2007 - scripts.iucr.org
     
    7. Shotgun crystallization strategy for structural genomics II: crystallization conditions that produce high resolution structures for T. maritima proteins
    R Page, AM Deacon, SA Lesley - Journal of structural and , 2005 - Springer
     
    8. Crystal structure of a type II quinolic acid phosphoribosyltransferase (TM1645) from Thermotoga maritima at 2.50 resolution
    R Schwarzenbacher, L Jaroszewski - Proteins: Structure, , 2004 - Wiley Online Library
     
    9. Structural and kinetic characterization of quinolinate phosphoribosyltransferase (hQPRTase) from Homo sapiens
    H Liu, K Woznica, G Catton, A Crawford - Journal of molecular , 2007 - Elsevier
     
    10. Walking through the protein sequence space: Towards new generation of the homology modeling
    ZM Frenkel, EN Trifonov - PROTEINS: Structure, Function, and , 2007 - Wiley Online Library
     
    11. Comprehensive X-ray Structural Studies of the Quinolinate Phosphoribosyl Transferase (BNA6) from Saccharomyces cerevisiae
    E di Luccio, DK Wilson - Biochemistry, 2008 - ACS Publications
     
    12. Subunit interfaces of oligomeric hyperthermophilic enzymes display enhanced compactness
    F Baldasseroni, S Pascarella - International journal of biological , 2009 - Elsevier
     
    13. A novel predicting algorithm of thermostable proteins based on choquet integral with respect to L-measure and hurst exponent
    JI Shieh, YL Liu, KJ Lee, PC Chang - Machine Learning and , 2009 - ieeexplore.ieee.org
     
    14. Carbohydrate utilization pathway analysis in the hyperthermophile Thermotoga maritima
    SB Conners - 2006 - repository.lib.ncsu.edu
     

    Protein Summary

    The TM1645 gene from Thermotoga maritima encodes the NP_229445 protein, a type II quinolic acid phosphoribosyltransferase (QAPRTase, NadC, EC:2.4.2.19, PubMed:15103640), which is an essential enzyme in the NAD+ biosynthetic pathway. This enzyme catalyzes the transfer of a phosphoribosyl moiety from 5-phosphoribosyl-1-pyrophosphate (PRPP) to quinolinic acid (QA), yielding nicotinic acid mononucleotide (NAMN), pyrophosphate and CO2, the last resulting from decarboxylation at position 2 of the quinolinate ring.

    The active enzyme exists as a dimer, where each monomer has two domains with different fold. The N-terminal domain (PF02749) has alpha/beta-Hammerhead fold (SCOP sunid:54664) and belongs to the family of quinolinic acid phosphoribosyltransferase N-terminal domain (SCOP sunid: 54676). The C-terminal domain (PF01729) has a TIM beta/alpha-barrel fold (SCOP sunid:51350) and belongs to a superfamily with characteristic incomplete beta/alpha barrel with parallel beta-sheet of 7 strands (Quinolinic acid phosphoribosyltransferase C-terminal domain; SCOP sunid:51690). DALI top hits are with other pyrophosphorylases like PDB:2jbm (Z=30), PDB:2b7n (Z=28), PDB:3l0g (Z=28), PDB:1x1o (Z=28).

    Ligand Summary



    References

    Reviews

    References

     

    No references found.

    Tag page

    Files (0)

     
    You must login to post a comment.
    All content on this site is licensed under a Creative Commons Attribution 3.0 License
    Powered by MindTouch