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1x2g

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(New page: 200px<br /><applet load="1x2g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x2g, resolution 2.40&Aring;" /> '''Crystal Structure of...)
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[[Image:1x2g.gif|left|200px]]<br /><applet load="1x2g" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1x2g, resolution 2.40&Aring;" />
 
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'''Crystal Structure of Lipate-Protein Ligase A from Escherichia coli'''<br />
 
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==Overview==
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==Crystal Structure of Lipate-Protein Ligase A from Escherichia coli==
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Lipoate-protein ligase A (LplA) catalyzes the formation of lipoyl-AMP from, lipoate and ATP and then transfers the lipoyl moiety to a specific lysine, residue on the acyltransferase subunit of alpha-ketoacid dehydrogenase, complexes and on H-protein of the glycine cleavage system. The, lypoyllysine arm plays a pivotal role in the complexes by shuttling the, reaction intermediate and reducing equivalents between the active sites of, the components of the complexes. We have determined the X-ray crystal, structures of Escherichia coli LplA alone and in a complex with lipoic, acid at 2.4 and 2.9 angstroms resolution, respectively. The structure of, LplA consists of a large N-terminal domain and a small C-terminal domain., The structure identifies the substrate binding pocket at the interface, between the two domains. Lipoic acid is bound in a hydrophobic cavity in, the N-terminal domain through hydrophobic interactions and a weak hydrogen, bond between carboxyl group of lipoic acid and the Ser-72 or Arg-140, residue of LplA. No large conformational change was observed in the main, chain structure upon the binding of lipoic acid.
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<StructureSection load='1x2g' size='340' side='right'caption='[[1x2g]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1x2g]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X2G FirstGlance]. <br>
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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]] 2.4&#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=MSE:SELENOMETHIONINE'>MSE</scene></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=1x2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x2g OCA], [https://pdbe.org/1x2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x2g RCSB], [https://www.ebi.ac.uk/pdbsum/1x2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x2g ProSAT]</span></td></tr>
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</table>
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== Function ==
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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>
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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/x2/1x2g_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=1x2g ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Lipoate-protein ligase A (LplA) catalyzes the formation of lipoyl-AMP from lipoate and ATP and then transfers the lipoyl moiety to a specific lysine residue on the acyltransferase subunit of alpha-ketoacid dehydrogenase complexes and on H-protein of the glycine cleavage system. The lypoyllysine arm plays a pivotal role in the complexes by shuttling the reaction intermediate and reducing equivalents between the active sites of the components of the complexes. We have determined the X-ray crystal structures of Escherichia coli LplA alone and in a complex with lipoic acid at 2.4 and 2.9 angstroms resolution, respectively. The structure of LplA consists of a large N-terminal domain and a small C-terminal domain. The structure identifies the substrate binding pocket at the interface between the two domains. Lipoic acid is bound in a hydrophobic cavity in the N-terminal domain through hydrophobic interactions and a weak hydrogen bond between carboxyl group of lipoic acid and the Ser-72 or Arg-140 residue of LplA. No large conformational change was observed in the main chain structure upon the binding of lipoic acid.
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==About this Structure==
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Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site.,Fujiwara K, Toma S, Okamura-Ikeda K, Motokawa Y, Nakagawa A, Taniguchi H J Biol Chem. 2005 Sep 30;280(39):33645-51. Epub 2005 Jul 25. PMID:16043486<ref>PMID:16043486</ref>
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1X2G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1X2G OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site., Fujiwara K, Toma S, Okamura-Ikeda K, Motokawa Y, Nakagawa A, Taniguchi H, J Biol Chem. 2005 Sep 30;280(39):33645-51. Epub 2005 Jul 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16043486 16043486]
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</div>
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<div class="pdbe-citations 1x2g" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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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: Motokawa, Y.]]
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[[Category: Motokawa Y]]
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[[Category: Nakagawa, A.]]
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[[Category: Nakagawa A]]
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[[Category: Okamura-Ikeda, K.]]
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[[Category: Okamura-Ikeda K]]
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[[Category: Taniguchi, H.]]
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[[Category: Taniguchi H]]
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[[Category: Toma, S.]]
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[[Category: Toma S]]
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[[Category: lipoate-protein ligase]]
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[[Category: lipoic acid]]
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[[Category: post-translational modification]]
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[[Category: protein acylation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:48:31 2007''
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Current revision

Crystal Structure of Lipate-Protein Ligase A from Escherichia coli

PDB ID 1x2g

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