1qbq
From Proteopedia
(New page: 200px<br /><applet load="1qbq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qbq, resolution 2.4Å" /> '''STRUCTURE OF RAT FARN...) |
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| - | [[Image:1qbq.jpg|left|200px]]<br /><applet load="1qbq" size=" | + | [[Image:1qbq.jpg|left|200px]]<br /><applet load="1qbq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qbq, resolution 2.4Å" /> | caption="1qbq, resolution 2.4Å" /> | ||
'''STRUCTURE OF RAT FARNESYL PROTEIN TRANSFERASE COMPLEXED WITH A CVIM PEPTIDE AND ALPHA-HYDROXYFARNESYLPHOSPHONIC ACID.'''<br /> | '''STRUCTURE OF RAT FARNESYL PROTEIN TRANSFERASE COMPLEXED WITH A CVIM PEPTIDE AND ALPHA-HYDROXYFARNESYLPHOSPHONIC ACID.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystallographic structure of acetyl-Cys-Val-Ile-selenoMet-COOH and | + | The crystallographic structure of acetyl-Cys-Val-Ile-selenoMet-COOH and alpha-hydroxyfarnesylphosphonic acid (alphaHFP) complexed with rat farnesyl protein transferase (FPT) (space group P61, a = b = 174. 13 A, c = 69.71 A, alpha = beta = 90 degrees, gamma = 120 degrees, Rfactor = 21.8%, Rfree = 29.2%, 2.5 A resolution) is reported. In the ternary complex, the bound substrates are within van der Waals contact of each other and the FPT enzyme. alphaHFP binds in an extended conformation in the active-site cavity where positively charged side chains and solvent molecules interact with the phosphate moiety and aromatic side chains pack adjacent to the isoprenoid chain. The backbone of the bound CaaX peptide adopts an extended conformation, and the side chains interact with both FPT and alphaHFP. The cysteine sulfur of the bound peptide coordinates the active-site zinc. Overall, peptide binding and recognition appear to be dominated by side-chain interactions. Comparison of the structures of the ternary complex and unliganded FPT [Park, H., Boduluri, S., Moomaw, J., Casey, P., and Beese, L. (1997) Science 275, 1800-1804] shows that major rearrangements of several active site side chains occur upon substrate binding. |
==About this Structure== | ==About this Structure== | ||
| - | 1QBQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ZN, ACT, ACE and HFP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1QBQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=HFP:'>HFP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QBQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: alpha-alpha-barrel helical crescent]] | [[Category: alpha-alpha-barrel helical crescent]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:01 2008'' |
Revision as of 12:38, 21 February 2008
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STRUCTURE OF RAT FARNESYL PROTEIN TRANSFERASE COMPLEXED WITH A CVIM PEPTIDE AND ALPHA-HYDROXYFARNESYLPHOSPHONIC ACID.
Overview
The crystallographic structure of acetyl-Cys-Val-Ile-selenoMet-COOH and alpha-hydroxyfarnesylphosphonic acid (alphaHFP) complexed with rat farnesyl protein transferase (FPT) (space group P61, a = b = 174. 13 A, c = 69.71 A, alpha = beta = 90 degrees, gamma = 120 degrees, Rfactor = 21.8%, Rfree = 29.2%, 2.5 A resolution) is reported. In the ternary complex, the bound substrates are within van der Waals contact of each other and the FPT enzyme. alphaHFP binds in an extended conformation in the active-site cavity where positively charged side chains and solvent molecules interact with the phosphate moiety and aromatic side chains pack adjacent to the isoprenoid chain. The backbone of the bound CaaX peptide adopts an extended conformation, and the side chains interact with both FPT and alphaHFP. The cysteine sulfur of the bound peptide coordinates the active-site zinc. Overall, peptide binding and recognition appear to be dominated by side-chain interactions. Comparison of the structures of the ternary complex and unliganded FPT [Park, H., Boduluri, S., Moomaw, J., Casey, P., and Beese, L. (1997) Science 275, 1800-1804] shows that major rearrangements of several active site side chains occur upon substrate binding.
About this Structure
1QBQ is a Protein complex structure of sequences from Rattus norvegicus with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue., Strickland CL, Windsor WT, Syto R, Wang L, Bond R, Wu Z, Schwartz J, Le HV, Beese LS, Weber PC, Biochemistry. 1998 Nov 24;37(47):16601-11. PMID:9843427
Page seeded by OCA on Thu Feb 21 14:38:01 2008
Categories: Protein complex | Rattus norvegicus | Beese, L. S. | Bond, R. | Le, H. V. | Schwartz, J. | Strickland, C. L. | Syto, R. | Wang, L. | Weber, P. C. | Windsor, W. T. | Wu, Z. | ACE | ACT | HFP | ZN | Alpha-alpha-barrel helical crescent
