PDBsum entry: 2azl

Transferase

PDB id: 2azl

Contents

Protein chain

279 a.a. *

Waters ×287

* Residue conservation analysis

PDB id:

2azl

Name:

Transferase

Title:

Crystal structure for the mutant f117e of thermotoga maritim octaprenyl pyrophosphate synthase

Structure:

Octoprenyl-diphosphate synthase. Chain: a. Synonym: octaprenyl pyrophosphate synthase. Engineered: yes. Mutation: yes

Source:

Thermotoga maritima. Organism_taxid: 2336. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Dimer (from PQS)

Resolution:

2.80Å R-factor: 0.223 R-free: 0.276

Authors:

H.Y.Sun,T.P.Ko,C.J.Kuo,R.T.Guo,C.C.Chou,P.H.Liang,A.H.Wang

Key ref:

H.Y.Sun et al. (2005). Homodimeric hexaprenyl pyrophosphate synthase from the thermoacidophilic crenarchaeon Sulfolobus solfataricus displays asymmetric subunit structures. J Bacteriol, 187, 8137-8148. PubMed id: 16291686 DOI: 10.1128/JB.187.23.8137-8148.2005

Date:

12-Sep-05 Release date: 14-Mar-06

Protein chain

Q9X1M1  (Q9X1M1_THEMA) -  Octoprenyl-diphosphate synthase, putative

Seq: 299 a.a.

Struc: 279 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 

• Biological process: isoprenoid biosynthetic process (1 term)
• Biochemical function: transferase activity (1 term)

DOI no: 10.1128/JB.187.23.8137-8148.2005

J Bacteriol 187:8137-8148 (2005)

PubMed id: 16291686

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

H.Y.Sun, T.P.Ko, C.J.Kuo, R.T.Guo, C.C.Chou, P.H.Liang, A.H.Wang.

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.