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| | <StructureSection load='3a7r' size='340' side='right'caption='[[3a7r]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='3a7r' size='340' side='right'caption='[[3a7r]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <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> | + | <table><tr><td colspan='2'>[[3a7r]] is a 1 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=3A7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A7R FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</td></tr> |
| - | <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>
| + | <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> |
| - | <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>
| + | |
| | <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> | | <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 == |
| - | [[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>
| + | [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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fujiwara, K]] | + | [[Category: Fujiwara K]] |
| - | [[Category: Hosaka, H]] | + | [[Category: Hosaka H]] |
| - | [[Category: Adenylate-forming enzyme]]
| + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Lipoic acid]]
| + | |
| - | [[Category: Lipoyl]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
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.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Lipoate-protein ligase A (LplA) catalyzes the attachment of lipoic acid to lipoate-dependent enzymes by a two-step reaction: first the lipoate adenylation reaction and, second, the lipoate transfer reaction. We previously determined the crystal structure of Escherichia coli LplA in its unliganded form and a binary complex with lipoic acid (Fujiwara, K., Toma, S., Okamura-Ikeda, K., Motokawa, Y., Nakagawa, A., and Taniguchi, H. (2005) J Biol. Chem. 280, 33645-33651). Here, we report two new LplA structures, LplA.lipoyl-5'-AMP and LplA.octyl-5'-AMP.apoH-protein complexes, which represent the post-lipoate adenylation intermediate state and the pre-lipoate transfer intermediate state, respectively. These structures demonstrate three large scale conformational changes upon completion of the lipoate adenylation reaction: movements of the adenylate-binding and lipoate-binding loops to maintain the lipoyl-5'-AMP reaction intermediate and rotation of the C-terminal domain by about 180 degrees . These changes are prerequisites for LplA to accommodate apoprotein for the second reaction. The Lys(133) residue plays essential roles in both lipoate adenylation and lipoate transfer reactions. Based on structural and kinetic data, we propose a reaction mechanism driven by conformational changes.
Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A.,Fujiwara K, Maita N, Hosaka H, Okamura-Ikeda K, Nakagawa A, Taniguchi H J Biol Chem. 2010 Mar 26;285(13):9971-80. Epub 2010 Jan 19. PMID:20089862[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Green DE, Morris TW, Green J, Cronan JE Jr, Guest JR. Purification and properties of the lipoate protein ligase of Escherichia coli. Biochem J. 1995 Aug 1;309 ( Pt 3):853-62. PMID:7639702
- ↑ Fujiwara K, Maita N, Hosaka H, Okamura-Ikeda K, Nakagawa A, Taniguchi H. Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A. J Biol Chem. 2010 Mar 26;285(13):9971-80. Epub 2010 Jan 19. PMID:20089862 doi:10.1074/jbc.M109.078717
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