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The Open Protein Structure Annotation Network
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1o50

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References
    Title Crystal structure of a tandem cystathionine-beta-synthase (CBS) domain protein (TM0935) from Thermotoga maritima at 1.87 A resolution. Proteins 57 213-217 2004
    Site JCSG
    PDB Id 1o50 Target Id 282804
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1247,TM0935 Molecular Weight 16555.72 Da.
    Residues 145 Isoelectric Point 5.13
    Sequence mkvkdvcklislkptvveedtpieeivdriledpvtrtvyvardnklvgmipvmhllkvsgfhffgfip keelirssmkrliaknaseimldpvyvhmdtpleealklmidnniqempvvdekgeivgdlnsleilla lwkgrek
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.87 Rfree 0.25495
    Matthews' coefficent 2.40 Rfactor 0.19113
    Waters 214 Solvent Content 48.27

    Ligand Information
    Ligands
    Metals

    Jmol

     

    Protein Summary

    Gene TM0935 from Thermotoga maritima translates in the NP_228743 protein that folds into a tandem cystathionine-beta-synthase (CBS) domain (PF00571; COG0517). CBS domains are widely distributed in all divisions of life, in the form of fusions with various unrelated proteins, where they usually form tandem pairs of about 120 aa that folds into one domain with a beta-sandwich and 4 alpha-helices extending from one edge [Ref]. Analysis of the genome context of TM0935 indicates the possible functional linkage (score 0.87) with the 5-methylthioadenosine deaminase mtaD (TM0936).

    1o50 classifies inside the alpha+beta class, CBS-domain pair (super)family. DALI top hits are with CBS domain protein PDB:2rc3 (Z=16), the MJ0100 protein PDB:3kpc (Z=16), and the YQZB protein PDB:3fv6 (Z=16).

    Functions of CBS domains are related to its ability to bind adenosyl-containing molecules to serve as energy or redox status sensing modules (PubMed: [Ref], [Ref], [Ref]). Cystathionine beta-synthase (CBS-domain containing protein) may function in oxidative stress defense by trans-sulfuration pathway [Ref], where S-adenosylmethionine stabilizes cystathionine beta-synthase and modulates redox capacity [Ref].

    Ligand Summary



    References

    Reviews

    References

     

    1. Kozbial PZ and Mushegian AR Natural history of S-adenosylmethionine-binding proteins. BMC Struct Biol. 2005 Oct 14; 5:19 PubMed HubMed doi:10.1186/1472-6807-5-19 pmid:16225687.

       


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    2. Scott JW, Hawley SA, Green KA, Anis M, Stewart G, Scullion GA, Norman DG, and Hardie DG CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. J Clin Invest. 2004 Jan; 113(2):274-84 PubMed HubMed doi:10.1172/JCI19874 pmid:14722619.

       


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    3. Kemp BE Bateman domains and adenosine derivatives form a binding contract. J Clin Invest. 2004 Jan; 113(2):182-4 PubMed HubMed doi:10.1172/JCI20846 pmid:14722609.

       


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    4. Banerjee R and Zou CG Redox regulation and reaction mechanism of human cystathionine-beta-synthase: a PLP-dependent hemesensor protein. Arch Biochem Biophys. 2005 Jan 1; 433(1):144-56 PubMed HubMed doi:10.1016/j.abb.2004.08.037 pmid:15581573.

       


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    5. Persa C, Osmotherly K, Chao-Wei Chen K, Moon S, and Lou MF The distribution of cystathionine beta-synthase (CBS) in the eye: implication of the presence of a trans-sulfuration pathway for oxidative stress defense. Exp Eye Res. 2006 Oct; 83(4):817-23 PubMed HubMed doi:10.1016/j.exer.2006.04.001 pmid:16769053.

       


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    6. Prudova A, Bauman Z, Braun A, Vitvitsky V, Lu SC, and Banerjee R S-adenosylmethionine stabilizes cystathionine beta-synthase and modulates redox capacity. Proc Natl Acad Sci U S A. 2006 Apr 25; 103(17):6489-94 PubMed HubMed doi:10.1073/pnas.0509531103 pmid:16614071.

       


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