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

    Title Crystal structure of ATP synthase subunit alpha (TM1612) from Thermotoga maritima at 2.10 A resolution. To be published
    Site JCSG
    PDB Id 2r9v Target Id 283469
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1304,TM1612, 382410 Molecular Weight 56058.80 Da.
    Residues 503 Isoelectric Point 6.34
    Sequence mrinpgeitkvleekiksfeekidledtgkviqvgdgiarayglnkvmvselvefvetgvkgvafnlee dnvgiiilgeykdikeghtvrrlkriievpvgeellgrvvnplgepldgkgpinaknfrpieikapgvi yrkpvdtplqtgikaidsmipigrgqreliigdrqtgktaiaidtiinqkgqgvyciyvaigqkksaia riidklrqygameyttvvvasasdpaslqyiapyagcamgeyfaysgrdalvvyddlskhavayrqlsl lmrrppgreaypgdifylhsrlleravrlndklgggsltalpivetqandisayiptnvisitdgqiyl epglfyagqrpainvglsvsrvggsaqikamkqvagmlridlaqyreletfaqfateldpatraqiirg qrlmellkqeqyspmpveeqvvvlfagvrgylddlpveevrrfekeflrfmhekhqdilddiktkkelt seteeklkkaieefkttfrv
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.10 Rfree 0.215
    Matthews' coefficent 4.48 Rfactor 0.180
    Waters 465 Solvent Content 72.54

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

    Ligand Information


    Google Scholar output for 2r9v
    1. Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard
    TC Terwilliger, PD Adams, RJ Read - Section D: Biological , 2009 - scripts.iucr.org

    Protein Summary

    This target is the alpha chain of F1-ATPase. There are abundant structural coverage for this target with high sequence similarity (~70% seq identity). However, there are no structures with alpha chain only. The F1-ATPase beta chain is similar to alpha chain (both seq and structurally) and contains the active site. The alpha chain also binds ATP and Mg (eg 1e79).

    It contains 3 domains (1-16 disordered):
    Domain 1: 17-96 all beta barrel,
    Domain 2: 97-372 P-loop containing nucleoside triphosphate hydrolases
    Domain 3: 373-503 left hand superhelix

    Although the structure is not unique, it is interesting in two aspects:

    a) first alpha chain in solution, ATP binds to alpha chain in monomer state;
    b) there are significant structure changes between 1st domain and 2/3 domains when compared monomeric alpha with alpha in complex form, this may be significant since the 1st domain is important in forming hetero-hexameric ring.

    It will be interesting to see complex structures with TM1609-1616 (alpha+beta, alpha+beta+gamma, etc).

    Homolog structures: 1sky, 1bmf, 1nbm, 1qo1, 1e1q, 1e1r, 1e79,1h8h

    Ligand Summary





    No references found.

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