1n4r

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Revision as of 19:50, 20 November 2007

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spinqualitylabelsall models 1n4r, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Protein Geranylgeranyltransferase type-I Complexed with a Geranylgeranylated KKKSKTKCVIL Peptide Product

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

1N4R is a Protein complex structure of sequences from Rattus norvegicus with ZN, CL, SO4, MES and TTH 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

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