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    Dr. Ann West gave a guest lecture on protein x-ray crystallography and its impact on signal transduction research. She discussed two-component signal transduction systems in bacteria where a stimulus leads to phosphorylation of a receptor which then phosphorylates a protein kinase. This kinase can auto-phosphorylate or phosphorylate other molecules to regulate responses. She presented the structure of the YPD1 protein from yeast, which forms a four-helix bundle with its phosphorylation site on helix alphaC. Phosphorylation causes a conformational change allowing the histidine and aspartic acid residues required for phosphorylation to interact.

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    Dr. Ann West gave a guest lecture on protein x-ray crystallography and its impact on signal transduction research. She discussed two-component signal transduction systems in bacteria where a stimulus leads to phosphorylation of a receptor which then phosphorylates a protein kinase. This kinase can auto-phosphorylate or phosphorylate other molecules to regulate responses. She presented the structure of the YPD1 protein from yeast, which forms a four-helix bundle with its phosphorylation site on helix alphaC. Phosphorylation causes a conformational change allowing the histidine and aspartic acid residues required for phosphorylation to interact.

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    © All Rights Reserved
    Download as DOCX, PDF, TXT or read online from Scribd
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    10 views1 page

    Guest Lecture Notes

    Uploaded by

    Benjamin Burton
    Dr. Ann West gave a guest lecture on protein x-ray crystallography and its impact on signal transduction research. She discussed two-component signal transduction systems in bacteria where a stimulus leads to phosphorylation of a receptor which then phosphorylates a protein kinase. This kinase can auto-phosphorylate or phosphorylate other molecules to regulate responses. She presented the structure of the YPD1 protein from yeast, which forms a four-helix bundle with its phosphorylation site on helix alphaC. Phosphorylation causes a conformational change allowing the histidine and aspartic acid residues required for phosphorylation to interact.

    Copyright:

    © All Rights Reserved
    Download as DOCX, PDF, TXT or read online from Scribd
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    Download as docx, pdf, or txt
    of 1

    Dr.

    Ann West Guest Lecture


    Protein X-Ray Crystallography: The Impact of a Structural Biology Approach
    on Signal Transduction Research

    www.rcsb.org - Protein Data Bank


    Two-Component Signal Transduction
    o In bacteria and simple cells, not in higher animal life
    o Stimulus Receptor ATP/ADP Protein Kinase Regulator
    (on/off) Response; hydrolyze the phosphate to give off Pii and
    returns regulator to off
    o Kinases phosphorylate themselves or other molecules; when they
    phosphorylate themselves auto-phosphorylation
    o Phosphoryl proteins can take a phosphorylation from a membrane
    protein to a protein further upstream in the pathway
    o Aspartic Acid always relays phosphate to Histidine, vice versa
    YPD1 Protein (phosphoryl in yeast)
    o All helical, six alpha-helices
    o Four-helix bundle core
    o Phosphorylation site located in middle of helix alphaC
    Phosphorylation of relay protein changes conformation so that Histidine
    and Aspartic Acid align to interact

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