5JFQ
Geranylgeranyl Pyrophosphate Synthetase from archaeon Geoglobus acetivorans
Summary for 5JFQ
| Entry DOI | 10.2210/pdb5jfq/pdb |
| Descriptor | Geranylgeranyl Pyrophosphate Synthetase (2 entities in total) |
| Functional Keywords | geranylgeranyl pyrophosphate synthetase, hyperthermophilic, archaeon, oxidoreductase |
| Biological source | Geoglobus acetivorans |
| Total number of polymer chains | 2 |
| Total formula weight | 72500.69 |
| Authors | Petrova, T.,Boyko, K.M.,Nikolaeva, A.Y.,Stekhanova, T.N.,Mardanov, A.V.,Rakitin, A.L.,Ravin, N.V.,Popov, V.O. (deposition date: 2016-04-19, release date: 2017-05-24, Last modification date: 2024-01-10) |
| Primary citation | Petrova, T.E.,Boyko, K.M.,Nikolaeva, A.Y.,Stekhanova, T.N.,Gruzdev, E.V.,Mardanov, A.V.,Stroilov, V.S.,Littlechild, J.A.,Popov, V.O.,Bezsudnova, E.Y. Structural characterization of geranylgeranyl pyrophosphate synthase GACE1337 from the hyperthermophilic archaeon Geoglobus acetivorans. Extremophiles, 22:877-888, 2018 Cited by PubMed Abstract: A novel type 1 geranylgeranyl pyrophosphate synthase GACE1337 has been identified within the genome of a newly identified hyperthermophilic archaeon Geoglobus acetivorans. The enzyme has been cloned and over-expressed in Escherichia coli. The recombinant enzyme has been biochemically and structurally characterized. It is able to catalyze the synthesis of geranylgeranyl pyrophosphate as a major product and of farnesyl pyrophosphate in smaller amounts, as measured by gas chromatography-mass spectrometry at an elevated temperature of 60 °C. Its ability to produce two products is consistent with the fact that GACE1337 is the only short-chain isoprenyl diphosphate synthase in G. acetivorans. Attempts to crystallize the enzyme were successful only at 37 °C. The three-dimensional structure of GACE1337 was determined by X-ray diffraction to 2.5 Å resolution. A comparison of its structure with those of related enzymes revealed that the Geoglobus enzyme has the features of both type I and type III geranylgeranyl pyrophosphate synthases, which allow it to regulate the product length. The active enzyme is a dimer and has three aromatic amino acids, two Phe, and a Tyr, located in the hydrophobic cleft between the two subunits. It is proposed that these bulky residues play a major role in the synthetic reaction by controlling the product elongation. PubMed: 30062607DOI: 10.1007/s00792-018-1044-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.51 Å) |
Structure validation
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