1n4q
From Proteopedia
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|PDB= 1n4q |SIZE=350|CAPTION= <scene name='initialview01'>1n4q</scene>, resolution 2.40Å | |PDB= 1n4q |SIZE=350|CAPTION= <scene name='initialview01'>1n4q</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MGM:2-[METHYL-(5-GERANYL-4-METHYL-PENT-3-ENYL)-AMINO]-ETHYL-DIPHOSPHATE'>MGM</scene>, <scene name='pdbligand=TTH:2,6,10,14-TETRAMETHYL-HEXADECA-2,6,10,14-TETRAENE'>TTH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1d8d|1D8D]], [[1fpp|1FPP]], [[1ft1|1FT1]], [[1kzo|1KZO]], [[1kzp|1KZP]], [[1qbq|1QBQ]], [[1dce|1DCE]], [[1n4p|1N4P]], [[1n4r|1N4R]], [[1n4s|1N4S]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4q OCA], [http://www.ebi.ac.uk/pdbsum/1n4q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n4q RCSB]</span> | ||
}} | }} | ||
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[[Category: Reid, T S.]] | [[Category: Reid, T S.]] | ||
[[Category: Taylor, J S.]] | [[Category: Taylor, J S.]] | ||
- | [[Category: CL]] | ||
- | [[Category: MGM]] | ||
- | [[Category: TTH]] | ||
- | [[Category: ZN]] | ||
[[Category: caax]] | [[Category: caax]] | ||
[[Category: geranylgeranyl]] | [[Category: geranylgeranyl]] | ||
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[[Category: rap2b]] | [[Category: rap2b]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:25:20 2008'' |
Revision as of 19:25, 30 March 2008
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, resolution 2.40Å | |||||||
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Ligands: | , , , | ||||||
Related: | 1D8D, 1FPP, 1FT1, 1KZO, 1KZP, 1QBQ, 1DCE, 1N4P, 1N4R, 1N4S
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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
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