Literature summary for 2.5.1.58 extracted from

Park, H.W.; Boduluri, S.R.; Moomaw, J.F.; Casey, P.J.; Beese, L.S.
Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution (1997), Science, 275, 1800-1804.

Search for more literature for 2.5.1.58

Application

Application	Comment	Organism
medicine	-	Rattus norvegicus

Cloned(Commentary)

Cloned (Comment)	Organism
enzyme produced using an Sf9 cell overexpression	Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment)	Organism
at 2.25 Angstrom, zinc occurs at a junction between a hydrophilic surface groove near the subunit interface: peptide binding site, and a deep lipophilic cleft in the beta subunit lined with aromatic residues: farnesyl diphosphate binding site	Rattus norvegicus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	zinc ion is coordinated by three residues in the beta subunit: Asp-297, Cys-299, and H-362 and a water molecule	Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
farnesyl diphosphate + protein-cysteine	Rattus norvegicus	-	S-farnesyl protein + diphosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
farnesyl diphosphate + protein-cysteine	posttranslational lipid modification in which a 15-carbon farnesyl isoprenoid is linked via a thioether bond to specific cysteine residues of proteins, the reactive cysteine is located in the C-terminal Ca1a2X motif in which C is the modified cysteine, a1 and a2 are often an aliphatic residue, and X is Ser, Met, Ala or Gln	Rattus norvegicus	diphosphate + S-farnesyl protein	-	?
farnesyl diphosphate + protein-cysteine	preferred CaaX-substrate: CAIM	Rattus norvegicus	diphosphate + S-farnesyl protein	-	?
farnesyl diphosphate + protein-cysteine	-	Rattus norvegicus	S-farnesyl protein + diphosphate	-	?

Subunits

Subunits	Comment	Organism
heterodimer	-	Rattus norvegicus

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Release 2023.1 (January 2023)