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3a7a

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==Crystal structure of E. coli lipoate-protein ligase A in complex with octyl-amp and apoH-protein==
==Crystal structure of E. coli lipoate-protein ligase A in complex with octyl-amp and apoH-protein==
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<StructureSection load='3a7a' size='340' side='right' caption='[[3a7a]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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<StructureSection load='3a7a' size='340' side='right'caption='[[3a7a]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3a7a]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A7A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A7A FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3a7a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A7A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A7A 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=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</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]] 3.1&#8491;</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]], [[3a7l|3a7l]], [[3a7r|3a7r]]</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=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene></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=562 Escherichia coli]), gcvH, b2904, JW2872 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=3a7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a7a OCA], [https://pdbe.org/3a7a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a7a RCSB], [https://www.ebi.ac.uk/pdbsum/3a7a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a7a ProSAT]</span></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=3a7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a7a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a7a RCSB], [http://www.ebi.ac.uk/pdbsum/3a7a PDBsum]</span></td></tr>
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</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> [[http://www.uniprot.org/uniprot/GCSH_ECOLI GCSH_ECOLI]] The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.[HAMAP-Rule:MF_00272]
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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]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/3a7a_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/3a7a_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=3a7a ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 3a7a" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Escherichia coli K-12]]
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[[Category: Fujiwara, K]]
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[[Category: Large Structures]]
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[[Category: Hosaka, H]]
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[[Category: Fujiwara K]]
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[[Category: Nakagawa, A]]
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[[Category: Hosaka H]]
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[[Category: Adeniylate-forming enzyme]]
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[[Category: Nakagawa A]]
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[[Category: Atp-binding]]
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[[Category: Ligase]]
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[[Category: Lipoyl]]
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[[Category: Nucleotide-binding]]
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[[Category: Transferase]]
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Current revision

Crystal structure of E. coli lipoate-protein ligase A in complex with octyl-amp and apoH-protein

PDB ID 3a7a

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