1rqc

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[[Image:1rqc.gif|left|200px]]
 
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{{Structure
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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==
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|PDB= 1rqc |SIZE=350|CAPTION= <scene name='initialview01'>1rqc</scene>, resolution 2.80&Aring;
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<StructureSection load='1rqc' size='340' side='right'caption='[[1rqc]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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<table><tr><td colspan='2'>[[1rqc]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RQC FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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|GENE= PDF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 Plasmodium falciparum])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqc OCA], [https://pdbe.org/1rqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rqc RCSB], [https://www.ebi.ac.uk/pdbsum/1rqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqc ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1rl4|1RL4]], [[1jym|1JYM]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqc OCA], [http://www.ebi.ac.uk/pdbsum/1rqc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rqc RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/Q8I372_PLAF7 Q8I372_PLAF7]
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== Evolutionary Conservation ==
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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'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rq/1rqc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rqc ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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.
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.
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==About this Structure==
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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<ref>PMID:15010544</ref>
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1RQC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQC OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15010544 15010544]
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</div>
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<div class="pdbe-citations 1rqc" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Plasmodium falciparum]]
[[Category: Plasmodium falciparum]]
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[[Category: Single protein]]
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[[Category: Hirsh I]]
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[[Category: Hirsh, I.]]
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[[Category: Hol WG]]
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[[Category: Hol, W G.]]
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[[Category: Kumar A]]
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[[Category: Kumar, A.]]
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[[Category: Nguyen KT]]
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[[Category: Nguyen, K T.]]
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[[Category: Pei D]]
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[[Category: Pei, D.]]
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[[Category: Robien MA]]
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[[Category: Robien, M A.]]
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[[Category: Turley S]]
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[[Category: Turley, S.]]
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[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:31:37 2008''
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Current revision

Crystals of peptide deformylase from Plasmodium falciparum with ten subunits per asymmetric unit reveal critical characteristics of the active site for drug design

PDB ID 1rqc

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