1n4q
From Proteopedia
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Protein Geranylgeranyltransferase type-I Complexed with a GGPP Analog and a KKKSKTKCVIL Peptide
Overview
Protein geranylgeranyltransferase type-I (GGTase-I), one of two CaaX, prenyltransferases, is an essential enzyme in eukaryotes. GGTase-I, catalyzes C-terminal lipidation of >100 proteins, including many GTP-, binding regulatory proteins. We present the first structural information, for mammalian GGTase-I, including a series of substrate and product, complexes that delineate the path of the chemical reaction. These, structures reveal that all protein prenyltransferases share a common, reaction mechanism and identify specific residues that play a dominant, role in determining prenyl group specificity. This hypothesis was, confirmed by converting farnesyltransferase (15-C prenyl substrate) into, GGTase-I (20-C prenyl substrate) with a single point mutation. GGTase-I, discriminates against farnesyl diphosphate (FPP) at the product turnover, step through the inability of a 15-C FPP to displace the 20-C, prenyl-peptide product. Understanding these key features of specificity is, expected to contribute to optimization of anti-cancer and anti-parasite, drugs.
About this Structure
1N4Q is a Protein complex structure of sequences from Rattus norvegicus with ZN, CL, TTH and MGM as ligands. Full crystallographic information is available from OCA.
Reference
Structure of mammalian protein geranylgeranyltransferase type-I., Taylor JS, Reid TS, Terry KL, Casey PJ, Beese LS, EMBO J. 2003 Nov 17;22(22):5963-74. PMID:14609943
Page seeded by OCA on Tue Nov 20 21:57:38 2007
