1n4q
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1n4q.gif|left|200px]] | [[Image:1n4q.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1n4q", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1n4q| PDB=1n4q | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Protein Geranylgeranyltransferase type-I Complexed with a GGPP Analog and a KKKSKTKCVIL Peptide''' | '''Protein Geranylgeranyltransferase type-I Complexed with a GGPP Analog and a KKKSKTKCVIL Peptide''' | ||
| Line 29: | Line 26: | ||
[[Category: Reid, T S.]] | [[Category: Reid, T S.]] | ||
[[Category: Taylor, J S.]] | [[Category: Taylor, J S.]] | ||
| - | [[Category: | + | [[Category: Caax]] |
| - | [[Category: | + | [[Category: Geranylgeranyl]] |
| - | [[Category: | + | [[Category: Ggtase]] |
| - | [[Category: | + | [[Category: Lipid modification]] |
| - | [[Category: | + | [[Category: Protein geranylgeranyltransferase type-i]] |
| - | [[Category: | + | [[Category: Protein prenylation]] |
| - | [[Category: | + | [[Category: Rap2b]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:05:40 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:05, 2 May 2008
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. 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 Sat May 3 02:05:40 2008
