2e5a

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(New page: 200px<br /><applet load="2e5a" size="450" color="white" frame="true" align="right" spinBox="true" caption="2e5a, resolution 2.10&Aring;" /> '''Crystal Structure of...)
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[[Image:2e5a.jpg|left|200px]]<br /><applet load="2e5a" size="450" 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 MG, PO4, LAQ and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:57:27 2007''
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Current revision

Crystal Structure of Bovine Lipoyltransferase in Complex with Lipoyl-AMP

PDB ID 2e5a

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