3a7l

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{{Seed}}
 
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[[Image:3a7l.png|left|200px]]
 
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==Crystal structure of E. coli apoH-protein==
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The line below this paragraph, containing "STRUCTURE_3a7l", creates the "Structure Box" on the page.
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<StructureSection load='3a7l' size='340' side='right'caption='[[3a7l]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3a7l]] 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=3A7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A7L FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.3&#8491;</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=3a7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a7l OCA], [https://pdbe.org/3a7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a7l RCSB], [https://www.ebi.ac.uk/pdbsum/3a7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a7l ProSAT]</span></td></tr>
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{{STRUCTURE_3a7l| PDB=3a7l | SCENE= }}
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</table>
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== Function ==
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[https://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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== 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/a7/3a7l_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=3a7l 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 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.
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===Crystal structure of E. coli apoH-protein===
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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<ref>PMID:20089862</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20089862}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3a7l" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20089862 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20089862}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia coli K-12]]
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3A7L is a 1 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=3A7L OCA].
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[[Category: Large Structures]]
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[[Category: Fujiwara K]]
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==Reference==
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[[Category: Maita N]]
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<ref group="xtra">PMID:20089862</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
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[[Category: Fujiwara, K.]]
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[[Category: Maita, N.]]
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[[Category: Glycine cleavage system]]
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[[Category: Lipoic acid]]
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[[Category: Lipoyl]]
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[[Category: Transport protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 7 10:00:39 2010''
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Current revision

Crystal structure of E. coli apoH-protein

PDB ID 3a7l

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