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==Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase) from Plasmodium falciparum in complex with TCMDC-124506==
==Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase) from Plasmodium falciparum in complex with TCMDC-124506==
<StructureSection load='4wi1' size='340' side='right' caption='[[4wi1]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='4wi1' size='340' side='right'caption='[[4wi1]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4wi1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WI1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WI1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4wi1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WI1 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3O6:1-(4-FLUOROPHENYL)-3-[4-(4-FLUOROPHENYL)-1-METHYL-3-(TRIFLUOROMETHYL)-1H-PYRAZOL-5-YL]UREA'>3O6</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ncx|4ncx]], [[4olf|4olf]], [[4q15|4q15]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3O6:1-(4-FLUOROPHENYL)-3-[4-(4-FLUOROPHENYL)-1-METHYL-3-(TRIFLUOROMETHYL)-1H-PYRAZOL-5-YL]UREA'>3O6</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proline--tRNA_ligase Proline--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.15 6.1.1.15] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wi1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wi1 OCA], [https://pdbe.org/4wi1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wi1 RCSB], [https://www.ebi.ac.uk/pdbsum/4wi1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wi1 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wi1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wi1 OCA], [http://pdbe.org/4wi1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wi1 RCSB], [http://www.ebi.ac.uk/pdbsum/4wi1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wi1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SYP_PLAF7 SYP_PLAF7]] Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro) (By similarity). Functions in trans to edit the amino acid moiety from incorrectly charged Ala-tRNA(Pro). Has no activity on correctly charged Pro-tRNA(Pro) or Ala-tRNA(Ala).<ref>PMID:14663147</ref>
[https://www.uniprot.org/uniprot/SYP_PLAF7 SYP_PLAF7] Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro) (By similarity). Functions in trans to edit the amino acid moiety from incorrectly charged Ala-tRNA(Pro). Has no activity on correctly charged Pro-tRNA(Pro) or Ala-tRNA(Ala).<ref>PMID:14663147</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4wi1" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4wi1" style="background-color:#fffaf0;"></div>
==See Also==
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Proline--tRNA ligase]]
[[Category: Large Structures]]
[[Category: Structural genomic]]
[[Category: Plasmodium falciparum 3D7]]
[[Category: Ligase]]
[[Category: Plasmodium falciparum]]
[[Category: Proline--trna ligase]]
[[Category: Prolyl-trna synthetase]]
[[Category: Pror]]
[[Category: Ssgcid]]

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