1rqc
From Proteopedia
(New page: 200px<br /><applet load="1rqc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rqc, resolution 2.80Å" /> '''Crystals of peptide ...) |
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| - | [[Image:1rqc.gif|left|200px]]<br /><applet load="1rqc" size=" | + | [[Image:1rqc.gif|left|200px]]<br /><applet load="1rqc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rqc, resolution 2.80Å" /> | caption="1rqc, resolution 2.80Å" /> | ||
'''Crystals of peptide deformylase from Plasmodium falciparum with ten subunits per asymmetric unit reveal critical characteristics of the active site for drug design'''<br /> | '''Crystals of peptide deformylase from Plasmodium falciparum with ten subunits per asymmetric unit reveal critical characteristics of the active site for drug design'''<br /> | ||
==Overview== | ==Overview== | ||
| - | An altered version of peptide deformylase from Plasmodium falciparum | + | An altered version of peptide deformylase from Plasmodium falciparum (PfPDF), the organism that causes the most devastating form of malaria, has been cocrystallized with a synthesized inhibitor that has submicromolar affinity for its target protein. The structure is solved at 2.2 A resolution, an improvement over the 2.8 A resolution achieved during the structural determination of unliganded PfPDF. This represents the successful outcome of modifying the protein construct in order to overcome adverse crystal contacts and other problems encountered in the study of unliganded PfPDF. Two molecules of PfPDF are found in the asymmetric unit of the current structure. The active site of each monomer of PfPDF is occupied by a proteolyzed fragment of the tripeptide-like inhibitor. Unexpectedly, each PfPDF subunit is associated with two nearly complete molecules of the inhibitor, found at a protein-protein interface. This is the first structure of a eukaryotic PDF protein, a potential drug target, in complex with a ligand. |
==About this Structure== | ==About this Structure== | ||
| - | 1RQC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] with CO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1RQC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] with <scene name='pdbligand=CO:'>CO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hirsh, I.]] | [[Category: Hirsh, I.]] | ||
| - | [[Category: Hol, W | + | [[Category: Hol, W G.]] |
[[Category: Kumar, A.]] | [[Category: Kumar, A.]] | ||
| - | [[Category: Nguyen, K | + | [[Category: Nguyen, K T.]] |
[[Category: Pei, D.]] | [[Category: Pei, D.]] | ||
| - | [[Category: Robien, M | + | [[Category: Robien, M A.]] |
[[Category: Turley, S.]] | [[Category: Turley, S.]] | ||
[[Category: CO]] | [[Category: CO]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:30 2008'' |
Revision as of 12:53, 21 February 2008
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Crystals of peptide deformylase from Plasmodium falciparum with ten subunits per asymmetric unit reveal critical characteristics of the active site for drug design
Overview
An altered version of peptide deformylase from Plasmodium falciparum (PfPDF), the organism that causes the most devastating form of malaria, has been cocrystallized with a synthesized inhibitor that has submicromolar affinity for its target protein. The structure is solved at 2.2 A resolution, an improvement over the 2.8 A resolution achieved during the structural determination of unliganded PfPDF. This represents the successful outcome of modifying the protein construct in order to overcome adverse crystal contacts and other problems encountered in the study of unliganded PfPDF. Two molecules of PfPDF are found in the asymmetric unit of the current structure. The active site of each monomer of PfPDF is occupied by a proteolyzed fragment of the tripeptide-like inhibitor. Unexpectedly, each PfPDF subunit is associated with two nearly complete molecules of the inhibitor, found at a protein-protein interface. This is the first structure of a eukaryotic PDF protein, a potential drug target, in complex with a ligand.
About this Structure
1RQC is a Single protein structure of sequence from Plasmodium falciparum with as ligand. Full crystallographic information is available from OCA.
Reference
An improved crystal form of Plasmodium falciparum peptide deformylase., Robien MA, Nguyen KT, Kumar A, Hirsh I, Turley S, Pei D, Hol WG, Protein Sci. 2004 Apr;13(4):1155-63. Epub 2004 Mar 9. PMID:15010544
Page seeded by OCA on Thu Feb 21 14:53:30 2008
Categories: Plasmodium falciparum | Single protein | Hirsh, I. | Hol, W G. | Kumar, A. | Nguyen, K T. | Pei, D. | Robien, M A. | Turley, S. | CO | Hydrolase
