1XTV

Sulfolobus solfataricus uracil phosphoribosyltransferase with uridine 5'-monophosphate (UMP) bound to half of the subunits

1XTV の概要

• エントリーDOI: 10.2210/pdb1xtv/pdb
• 関連するPDBエントリー: 1XTT 1XTU
• 分子名称: Probable uracil phosphoribosyltransferase, URIDINE-5'-MONOPHOSPHATE (2 entities in total)
• 機能のキーワード: tetramer, type 1 phosphoribosyltransferase, ump complex, transferase
• 由来する生物種: Sulfolobus solfataricus
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 194731.51

構造登録者

Arent, S.,Harris, P.,Jensen, K.F.,Larsen, S. (登録日: 2004-10-24, 公開日: 2005-02-08, 最終更新日: 2023-10-25)

主引用文献

Arent, S.,Harris, P.,Jensen, K.F.,Larsen, S.
Allosteric Regulation and Communication between Subunits in Uracil Phosphoribosyltransferase from Sulfolobus solfataricus(,)
Biochemistry, 44:883-892, 2005

PubMed Abstract: Uracil phosphoribosyltransferase (UPRTase) catalyzes the conversion of 5-phosphate-alpha-1-diphosphate (PRPP) and uracil to uridine 5'-monophosphate (UMP) and diphosphate. The UPRTase from Sulfolobus solfataricus has a unique regulation by nucleoside triphosphates compared to UPRTases from other organisms. To understand the allosteric regulation, crystal structures were determined for S. solfataricus UPRTase in complex with UMP and with UMP and the allosteric inhibitor CTP. Also, a structure with UMP bound in half of the active sites was determined. All three complexes form tetramers but reveal differences in the subunits and their relative arrangement. In the UPRTase-UMP complex, the peptide bond between a conserved arginine residue (Arg80) and the preceding residue (Leu79) adopts a cis conformation in half of the subunits and a trans conformation in the other half and the tetramer comprises two cis-trans dimers. In contrast, four identical subunits compose the UPRTase-UMP-CTP tetramer. CTP binding affects the conformation of Arg80, and the Arg80 conformation in the UPRTase-UMP-CTP complex leaves no room for binding of the substrate PRPP. The different conformations of Arg80 coupled to rearrangements in the quaternary structure imply that this residue plays a major role in regulation of the enzyme and in communication between subunits. The ribose ring of UMP adopts alternative conformations in the cis and trans subunits of the UPRTase-UMP tetramer with associated differences in the interactions of the catalytically important Asp209. The active-site differences have been related to proposed kinetic models and provide an explanation for the regulatory significance of the C-terminal Gly216.

PubMed: 15654744
DOI: 10.1021/bi048041l

実験手法

X-RAY DIFFRACTION (2.6 Å)