Tubulin tyrosine ligase

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(New page: <StructureSection load='3tin' size='340' side='right' caption='Tubulin tyrosine ligase complex with ADP (PDB code 3tin)' scene=''> '''Tubulin tyrosine ligase''' (TTL) adds tyrosine in...)
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<StructureSection load='3tin' size='340' side='right' caption='Tubulin tyrosine ligase complex with ADP (PDB code [[3tin]])' scene=''>
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'''Tubulin tyrosine ligase''' (TTL) adds tyrosine in an ATP-dependent reaction to the C-terminal of a detyrosinated a-tubulin. The detyrosination of a-tubulin is a posttranslational modification which exposes glutamate in the new tubulin C-terminal. The detyrosinated a-tubulin forms Glu-microtubules.
'''Tubulin tyrosine ligase''' (TTL) adds tyrosine in an ATP-dependent reaction to the C-terminal of a detyrosinated a-tubulin. The detyrosination of a-tubulin is a posttranslational modification which exposes glutamate in the new tubulin C-terminal. The detyrosinated a-tubulin forms Glu-microtubules.

Revision as of 08:07, 20 July 2015

Tubulin tyrosine ligase complex with ADP and Mg+2 ions (PDB code 3tin)

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3D Structures of tubulin tyrosine ligase

Updated on 20-July-2015


3tig – fTTL - frog
3tii – fTTL + phosphomethylphosphonic acid adenylate
3tin – fTTL + ADP
4iij – cTTL + rSTM + tubulin + GTP + GDP - chicken
4ihj – cTTL + rSTM + tubulin + GTP + GDP + ADP
4wbn – cTTL + rSTM + tubulin + GTP + GDP + phosphomethylphosphonic acid adenylate
4o2a – cTTL + rSTM + tubulin + GTP + GDP + ADP + inhibitor
4i4t – cTTL + rSTM + tubulin + GTP + GDP + zampanolide
4i50 – cTTL + rSTM + tubulin + GTP + GDP + epothilone
4o4l, 4tuy, 4tv8, 4yj2, 4yj3 – cTTL + rSTM + tubulin + GTP + GDP + anti-cancer drugs
4i55 – cTTL + rSTM + tubulin + GTP + GDP + phosphomethylphosphonic acid adenylate
4o2b – cTTL + rSTM + tubulin + GTP + GDP + phosphomethylphosphonic acid adenylate + anti-gout drug
4o4h, 4o4j, 4o4i – cTTL + rSTM + tubulin + GTP + GDP + phosphomethylphosphonic acid adenylate + anti-cancer drug

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Joel L. Sussman, Alexander Berchansky

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