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5ifu

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Current revision (13:50, 30 August 2023) (edit) (undo)
 
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<StructureSection load='5ifu' size='340' side='right'caption='[[5ifu]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
<StructureSection load='5ifu' size='340' side='right'caption='[[5ifu]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ifu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plaf7 Plaf7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IFU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5IFU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ifu]] 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=5IFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IFU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GBM:5-CHLORO-N-(2-{4-[(CYCLOHEXYLCARBAMOYL)SULFAMOYL]PHENYL}ETHYL)-2-METHOXYBENZAMIDE'>GBM</scene></td></tr>
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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]] 2.45&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ncx|4ncx]], [[4q15|4q15]], [[4wi1|4wi1]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GBM:5-CHLORO-N-(2-{4-[(CYCLOHEXYLCARBAMOYL)SULFAMOYL]PHENYL}ETHYL)-2-METHOXYBENZAMIDE'>GBM</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">proRS, PFL0670c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</td></tr>
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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=5ifu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ifu OCA], [https://pdbe.org/5ifu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ifu RCSB], [https://www.ebi.ac.uk/pdbsum/5ifu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ifu ProSAT]</span></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ifu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ifu OCA], [http://pdbe.org/5ifu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ifu RCSB], [http://www.ebi.ac.uk/pdbsum/5ifu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ifu ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[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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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Plaf7]]
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[[Category: Plasmodium falciparum 3D7]]
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[[Category: Proline--tRNA ligase]]
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[[Category: Abendroth J]]
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[[Category: Abendroth, J]]
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[[Category: Dranow DM]]
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[[Category: Dranow, D M]]
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[[Category: Hewitt SN]]
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[[Category: Hewitt, S N]]
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[[Category: Structural genomic]]
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[[Category: Glyburide]]
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[[Category: Ligase]]
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[[Category: Plasmodium falciparum]]
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[[Category: Proline--trna ligase]]
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[[Category: Prolyl-trna synthetase]]
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[[Category: Pror]]
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[[Category: Sgc]]
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Current revision

Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase) from Plasmodium falciparum in complex with Glyburide

PDB ID 5ifu

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OCA

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