Homodimeric hexaprenyl pyrophosphate synthase from the thermoacidophilic crenarchaeon Sulfolobus solfataricus displays asymmetric subunit structures

Han Yu Sun, Tzu Ping Ko, Chih Jung Kuo, Rey Ting Guo, Chia Cheng Chou, Po Huang Liang, Andrew H.J. Wang

研究成果: 雜誌貢獻文章同行評審

27 引文 斯高帕斯(Scopus)

摘要

Hexaprenyl pyrophosphate synthase (HexPPs) from Sulfolobus solfataricus catalyzes the synthesis of trans-C30-hexaprenyl pyrophosphate (HexPP) by reacting two isopentenyl pyrophosphate molecules with one geranylgeranyl pyrophosphate. The crystal structure of the homodimeric C30-HexPPs resembles those of other trans-prenyltransferases, including farnesyl pyrophosphate synthase (FPPs) and octaprenyl pyrophosphate synthase (OPPs). In both subunits, 10 core helices are arranged about a central active site cavity. Leu164 in the middle of the cavity controls the product chain length. Two protein conformers are observed in the S. solfataricus HexPPs structure, and the major difference between them occurs in the flexible region of residues 84 to 100. Several helices (αI, αJ, αK, and part of αH) and the associated loops have high-temperature factors in one monomer, which may be related to the domain motion that controls the entrance to the active site. Different side chain conformations of Trp136 in two HexPPs subunits result in weaker hydrophobic interactions at the dimer interface, in contrast to the symmetric π-π stacking interactions of aromatic side chains found in FPPs and OPPs. Finally, the three-conformer switched model may explain the catalytic process for HexPPs.

原文英語
頁(從 - 到)8137-8148
頁數12
期刊Journal of Bacteriology
187
發行號23
DOIs
出版狀態已發佈 - 12月 2005
對外發佈

ASJC Scopus subject areas

  • 微生物學
  • 分子生物學

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