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3a7r

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==Crystal structure of E. coli lipoate-protein ligase A in complex with lipoyl-AMP.==
==Crystal structure of E. coli lipoate-protein ligase A in complex with lipoyl-AMP.==
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<StructureSection load='3a7r' size='340' side='right' caption='[[3a7r]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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<StructureSection load='3a7r' size='340' side='right'caption='[[3a7r]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3a7r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A7R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A7R FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3a7r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A7R FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LAQ:5-O-[(R)-({5-[(3R)-1,2-DITHIOLAN-3-YL]PENTANOYL}OXY)(HYDROXY)PHOSPHORYL]ADENOSINE'>LAQ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=LAQ:5-O-[(R)-({5-[(3R)-1,2-DITHIOLAN-3-YL]PENTANOYL}OXY)(HYDROXY)PHOSPHORYL]ADENOSINE'>LAQ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1x2g|1x2g]], [[1x2h|1x2h]], [[2e5a|2e5a]], [[3a7a|3a7a]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1x2g|1x2g]], [[1x2h|1x2h]], [[2e5a|2e5a]], [[3a7a|3a7a]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lplA, yjjF, b4386, JW4349 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lplA, yjjF, b4386, JW4349 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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<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=3a7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a7r OCA], [http://pdbe.org/3a7r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a7r RCSB], [http://www.ebi.ac.uk/pdbsum/3a7r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a7r ProSAT]</span></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=3a7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a7r OCA], [https://pdbe.org/3a7r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a7r RCSB], [https://www.ebi.ac.uk/pdbsum/3a7r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a7r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/LPLA_ECOLI LPLA_ECOLI]] Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to catalyze very poorly the transfer of lipoyl and octanoyl moiety from their acyl carrier protein.<ref>PMID:7639702</ref>
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[[https://www.uniprot.org/uniprot/LPLA_ECOLI LPLA_ECOLI]] Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to catalyze very poorly the transfer of lipoyl and octanoyl moiety from their acyl carrier protein.<ref>PMID:7639702</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Ecoli]]
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[[Category: Large Structures]]
[[Category: Fujiwara, K]]
[[Category: Fujiwara, K]]
[[Category: Hosaka, H]]
[[Category: Hosaka, H]]

Revision as of 16:19, 22 December 2021

Crystal structure of E. coli lipoate-protein ligase A in complex with lipoyl-AMP.

PDB ID 3a7r

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