1USY

ATP phosphoribosyl transferase (HisG:HisZ) complex from Thermotoga maritima

Summary for 1USY

• Entry DOI: 10.2210/pdb1usy/pdb
• Descriptor: ATP PHOSPHORIBOSYLTRANSFERASE REGULATORY SUBUNIT, ATP PHOSPHORIBOSYLTRANSFERASE, HISTIDINE, ... (7 entities in total)
• Functional Keywords: transferase, atp phosphoribosyl transferase, aminoacyl-trna synthetase
• Biological source: THERMOTOGA MARITIMA; More
• Cellular location: Cytoplasm (By similarity): Q9X0D3 Q9X0D3 Q9X0D2 Q9X0D2
• Total number of polymer chains: 8
• Total formula weight: 221331.15

Authors

Vega, M.C.,Fernandez, F.J.,Murphy, G.E.,Zou, P.,Popov, A.,Wilmanns, M. (deposition date: 2003-12-01, release date: 2004-12-15, Last modification date: 2024-10-23)

Primary citation

Vega, M.C.,Zou, P.,Fernandez, F.J.,Murphy, G.E.,Sterner, R.,Popov, A.,Wilmanns, M.
Regulation of the Hetero-Octameric ATP Phosphoribosyl Transferase Complex from Thermotoga Maritima by a tRNA Synthetase-Like Subunit.
Mol.Microbiol., 55:675-, 2005

PubMed 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 for these findings is provided by the crystal structure revealing a total of eight histidine binding sites that are located within each of the four HisGS-HisZ subunit interfaces formed by the ATP phosphoribosyl transferase complex. While the structure of the catalytic HisGS subunit is related to the catalytic domain of another family of (HisGL)2 ATP phosphoribosyl transferases that is functional in the absence of additional regulatory subunits, the structure of the regulatory HisZ subunit is distantly related to class II aminoacyl-tRNA synthetases. However, neither the mode of the oligomeric subunit arrangement nor the type of histidine binding pockets is found in these structural relatives. Common ancestry of the regulatory HisZ subunit and class II aminoacyl-tRNA synthetase may reflect the balanced need of regulated amounts of a cognate amino acid (histidine) in the translation apparatus, ultimately linking amino acid biosynthesis and protein biosynthesis in terms of function, structure and evolution.

PubMed: 15660995
DOI: 10.1111/J.1365-2958.2004.04422.X

Experimental method

X-RAY DIFFRACTION (2.52 Å)