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| {{STRUCTURE_1n4s| PDB=1n4s | SCENE= }} | | {{STRUCTURE_1n4s| PDB=1n4s | SCENE= }} |
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| '''Protein Geranylgeranyltransferase type-I Complexed with GGPP and a Geranylgeranylated KKKSKTKCVIL Peptide Product'''
| | ===Protein Geranylgeranyltransferase type-I Complexed with GGPP and a Geranylgeranylated KKKSKTKCVIL Peptide Product=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14609943}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14609943 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14609943}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Protein prenylation]] | | [[Category: Protein prenylation]] |
| [[Category: Rap2b]] | | [[Category: Rap2b]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:05:48 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:44:37 2008'' |
