2e5a

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[[Image:2e5a.jpg|left|200px]]<br /><applet load="2e5a" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2e5a, resolution 2.10&Aring;" />
 
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'''Crystal Structure of Bovine Lipoyltransferase in Complex with Lipoyl-AMP'''<br />
 
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==Overview==
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==Crystal Structure of Bovine Lipoyltransferase in Complex with Lipoyl-AMP==
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Lipoic acid is an essential cofactor of the alpha-ketoacid dehydrogenase complexes and the glycine cleavage system. It is covalently attached to a specific lysine residue of the subunit of the complexes. The bovine lipoyltransferase (bLT) catalyzes the lipoic acid attachment reaction using lipoyl-AMP as a substrate, forming a lipoylated protein and AMP. To gain insights into the reaction mechanism at the atomic level, we have determined the crystal structure of bLT at 2.10 A resolution. Unexpectedly, the purified recombinant bLT contains endogenous lipoyl-AMP. The structure of bLT consists of N-terminal and C-terminal domains, and lipoyl-AMP is bound to the active site in the N-terminal domain, adopting a U-shaped conformation. The lipoyl moiety is buried in the hydrophobic pocket, forming van der Waals interactions, and the AMP moiety forms numerous hydrogen bonds with bLT in another tunnel-like cavity. These interactions work together to expose the C10 atom of lipoyl-AMP to the surface of the bLT molecule. The carbonyl oxygen atom of lipoyl-AMP interacts with the invariant Lys135. The interaction might stimulate the positive charge of the C10 atom of lipoyl-AMP, and consequently facilitate the nucleophilic attack by the lysine residue of the lipoate-acceptor protein, accompanying the bond cleavage between the carbonyl group and the phosphate group. We discuss the structural differences between bLT and the lipoate-protein ligase A from Escherichia coli and Thermoplasma acidophilum. We further demonstrate that bLT in mitochondria also contains endogenous lipoylmononucleotide, being ready for the lipoylation of apoproteins.
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<StructureSection load='2e5a' size='340' side='right'caption='[[2e5a]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2e5a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E5A FirstGlance]. <br>
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2E5A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=LAQ:'>LAQ</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E5A OCA].
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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]] 2.1&#8491;</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=ACY:ACETIC+ACID'>ACY</scene>, <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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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==Reference==
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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=2e5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e5a OCA], [https://pdbe.org/2e5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e5a RCSB], [https://www.ebi.ac.uk/pdbsum/2e5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e5a ProSAT]</span></td></tr>
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Crystal structure of bovine lipoyltransferase in complex with lipoyl-AMP., Fujiwara K, Hosaka H, Matsuda M, Okamura-Ikeda K, Motokawa Y, Suzuki M, Nakagawa A, Taniguchi H, J Mol Biol. 2007 Aug 3;371(1):222-34. Epub 2007 May 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17570395 17570395]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LIPT_BOVIN LIPT_BOVIN] Catalyzes the transfer of the lipoyl group from lipoyl-AMP to the specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e5/2e5a_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</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/main_output.php?pdb_ID=2e5a ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Fujiwara, K.]]
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[[Category: Fujiwara K]]
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[[Category: Hosaka, H.]]
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[[Category: Hosaka H]]
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[[Category: Matsuda, M.]]
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[[Category: Matsuda M]]
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[[Category: Nakagawa, A.]]
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[[Category: Nakagawa A]]
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[[Category: Suzuki, M.]]
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[[Category: Suzuki M]]
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[[Category: ACY]]
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[[Category: LAQ]]
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[[Category: MG]]
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[[Category: PO4]]
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[[Category: ligase]]
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[[Category: lipoyl-amp]]
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[[Category: lipoyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:06:27 2008''
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Current revision

Crystal Structure of Bovine Lipoyltransferase in Complex with Lipoyl-AMP

PDB ID 2e5a

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