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Guest Lecture Notes

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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Benjamin Burton
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17 views

Guest Lecture Notes

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.

Uploaded by

Benjamin Burton
Copyright
© © All Rights Reserved
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd
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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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