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TitleMultivalent Microtubule Recognition by Tubulin Tyrosine Ligase-like Family Glutamylases.
Journal, issue, pagesCell, Vol. 161, Issue 5, Page 1112-1123, Year 2015
Publish dateMay 21, 2015
AuthorsChristopher P Garnham / Annapurna Vemu / Elizabeth M Wilson-Kubalek / Ian Yu / Agnieszka Szyk / Gabriel C Lander / Ronald A Milligan / Antonina Roll-Mecak /
PubMed AbstractGlutamylation, the most prevalent tubulin posttranslational modification, marks stable microtubules and regulates recruitment and activity of microtubule- interacting proteins. Nine enzymes of the ...Glutamylation, the most prevalent tubulin posttranslational modification, marks stable microtubules and regulates recruitment and activity of microtubule- interacting proteins. Nine enzymes of the tubulin tyrosine ligase-like (TTLL) family catalyze glutamylation. TTLL7, the most abundant neuronal glutamylase, adds glutamates preferentially to the β-tubulin tail. Coupled with ensemble and single-molecule biochemistry, our hybrid X-ray and cryo-electron microscopy structure of TTLL7 bound to the microtubule delineates a tripartite microtubule recognition strategy. The enzyme uses its core to engage the disordered anionic tails of α- and β-tubulin, and a flexible cationic domain to bind the microtubule and position itself for β-tail modification. Furthermore, we demonstrate that all single-chain TTLLs with known glutamylase activity utilize a cationic microtubule-binding domain analogous to that of TTLL7. Therefore, our work reveals the combined use of folded and intrinsically disordered substrate recognition elements as the molecular basis for specificity among the enzymes primarily responsible for chemically diversifying cellular microtubules.
External linksCell / PubMed:25959773 / PubMed Central
MethodsEM (helical sym.) / X-ray diffraction
Resolution2.55 - 7.95 Å
Structure data

EMDB-6307:
Electron cryo-microscopy of microtubule-bound TTLL7
Method: EM (helical sym.) / Resolution: 7.95 Å

PDB-4ylr:
Tubulin Glutamylase
Method: X-RAY DIFFRACTION / Resolution: 2.55 Å

PDB-4yls:
Tubulin Glutamylase
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-HOH:
WATER / Water

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • homo sapiens (human)
  • Bos taurus (cattle)
KeywordsLIGASE / Enzyme

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