2AZK
Crystal structure for the mutant W136E of Sulfolobus solfataricus hexaprenyl pyrophosphate synthase
Summary for 2AZK
| Entry DOI | 10.2210/pdb2azk/pdb |
| Related | 2AZJ |
| Descriptor | Geranylgeranyl pyrophosphate synthetase (2 entities in total) |
| Functional Keywords | hexpps, trans-prenyltransferase, isoprenyl pyrophosphate synthase, transferase |
| Biological source | Sulfolobus solfataricus |
| Total number of polymer chains | 2 |
| Total formula weight | 66573.73 |
| Authors | Sun, H.Y.,Ko, T.P.,Kuo, C.J.,Guo, R.T.,Chou, C.C.,Liang, P.H.,Wang, A.H.J. (deposition date: 2005-09-12, release date: 2006-03-14, Last modification date: 2023-10-25) |
| Primary citation | Sun, H.Y.,Ko, T.P.,Kuo, C.J.,Guo, R.T.,Chou, C.C.,Liang, P.H.,Wang, A.H.J. Homodimeric hexaprenyl pyrophosphate synthase from the thermoacidophilic crenarchaeon Sulfolobus solfataricus displays asymmetric subunit structures J.Bacteriol., 187:8137-8148, 2005 Cited by PubMed Abstract: Hexaprenyl pyrophosphate synthase (HexPPs) from Sulfolobus solfataricus catalyzes the synthesis of trans-C(30)-hexaprenyl pyrophosphate (HexPP) by reacting two isopentenyl pyrophosphate molecules with one geranylgeranyl pyrophosphate. The crystal structure of the homodimeric C(30)-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 (alphaI, alphaJ, alphaK, and part of alphaH) 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. PubMed: 16291686DOI: 10.1128/JB.187.23.8137-8148.2005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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