2F6U

Crystal Structure of (S)-3-O-Geranylgeranylglyceryl Phosphate Synthase complexed with citrate

Summary for 2F6U

• Entry DOI: 10.2210/pdb2f6u/pdb
• Related: 1VIZ 2F6X
• Descriptor: (S)-3-O-Geranylgeranylglyceryl Phosphate Synthase, CITRIC ACID (3 entities in total)
• Functional Keywords: non-canonical tim-barrel; prenyltransferase; archaeal lipid synthesis; dimer, transferase
• Biological source: Archaeoglobus fulgidus
• Cellular location: Cytoplasm (By similarity): O29844
• Total number of polymer chains: 2
• Total formula weight: 53294.41

Authors

Payandeh, J. (deposition date: 2005-11-29, release date: 2006-01-24, Last modification date: 2024-04-03)

Primary citation

Payandeh, J.,Fujihashi, M.,Gillon, W.,Pai, E.F.
The crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase reveals an ancient fold for an ancient enzyme
J.Biol.Chem., 281:6070-6078, 2006

PubMed Abstract: We report crystal structures of the citrate and sn-glycerol-1-phosphate (G1P) complexes of (S)-3-O-geranylgeranylglyceryl phosphate synthase from Archaeoglobus fulgidus (AfGGGPS) at 1.55 and 2.0 A resolution, respectively. AfGGGPS is an enzyme that performs the committed step in archaeal lipid biosynthesis, and it presents the first triose phosphate isomerase (TIM)-barrel structure with a prenyltransferase function. Our studies provide insight into the catalytic mechanism of AfGGGPS and demonstrate how it selects for the sn-G1P isomer. The replacement of "Helix 3" by a "strand" in AfGGGPS, a novel modification to the canonical TIM-barrel fold, suggests a model of enzyme adaptation that involves a "greasy slide" and a "swinging door." We propose functions for the homologous PcrB proteins, which are conserved in a subset of pathogenic bacteria, as either prenyltransferases or being involved in lipoteichoic acid biosynthesis. Sequence and structural comparisons lead us to postulate an early evolutionary history for AfGGGPS, which may highlight its role in the emergence of Archaea.

PubMed: 16377641
DOI: 10.1074/jbc.M509377200

Experimental method

X-RAY DIFFRACTION (1.55 Å)