This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sun, H.-Y.
Right arrow Articles by Wang, A. H.-J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sun, H.-Y.
Right arrow Articles by Wang, A. H.-J.

 Previous Article  |  Next Article 

Journal of Bacteriology, December 2005, p. 8137-8148, Vol. 187, No. 23
0021-9193/05/$08.00+0     doi:10.1128/JB.187.23.8137-8148.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Homodimeric Hexaprenyl Pyrophosphate Synthase from the Thermoacidophilic Crenarchaeon Sulfolobus solfataricus Displays Asymmetric Subunit Structures{dagger}

Han-Yu Sun,1,2 Tzu-Ping Ko,2 Chih-Jung Kuo,2 Rey-Ting Guo,1,4 Chia-Cheng Chou,2,3 Po-Huang Liang,1,2,4 and Andrew H.-J. Wang1,2,3,4*

Institute of Biochemical Sciences, National Taiwan University, Taipei 106,1 Institute of Biological Chemistry,2 Core Facility for Protein X-Ray Crystallography,3 Taiwan International Graduate Program, Academia Sinica, Taipei 115, Taiwan4

Received 20 June 2005/ Accepted 26 August 2005

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 ({alpha}I, {alpha}J, {alpha}K, and part of {alpha}H) 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 {pi}-{pi} stacking interactions of aromatic side chains found in FPPs and OPPs. Finally, the three-conformer switched model may explain the catalytic process for HexPPs.

* Corresponding author. Mailing address: Institute of Biological Chemistry, Academia Sinica, 128 Academia Road, Taipei 115, Taiwan. Phone: 886-2-2788-1981. Fax: 886-2-2788-2043. E-mail: ahjwang{at}gate.sinica.edu.tw.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

Journal of Bacteriology, December 2005, p. 8137-8148, Vol. 187, No. 23
0021-9193/05/$08.00+0     doi:10.1128/JB.187.23.8137-8148.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Chang, T.-H., Guo, R.-T., Ko, T.-P., Wang, A. H.-J., Liang, P.-H. (2006). Crystal Structure of Type-III Geranylgeranyl Pyrophosphate Synthase from Saccharomyces cerevisiae and the Mechanism of Product Chain Length Determination. J. Biol. Chem. 281: 14991-15000 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»