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Regulation of the hetero-octameric ATP phosphoribosyl transferase complex from Thermotoga maritima by a tRNA synthetase-like subunit.

Vega, M. Cristina ; Zou, Peijian ; Fernandez, Francisco J. ; Murphy, Gavin E. ; Sterner, Reinhard ; Popov, Alexander ; Wilmanns, Matthias



Abstract

The molecular structure of the ATP phosphoribosyl transferase from the hyperthermophile Thermotoga maritima is composed of a 220 kDa hetero-octameric complex comprising four catalytic subunits (HisGS) and four regulatory subunits (HisZ). Steady-state kinetics indicate that only the complete octameric complex is active and non-competitively inhibited by the pathway product histidine. The rationale ...

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