3a8j: Difference between revisions

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-{{Seed}}
-[[Image:3a8j.jpg|left|200px]]
-<!--
+==Crystal Structure of ET-EHred complex==
-The line below this paragraph, containing "STRUCTURE_3a8j", creates the "Structure Box" on the page.
+<StructureSection load='3a8j' size='340' side='right'caption='[[3a8j]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3a8j]] is a 6 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=3A8J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A8J FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LA2:N~6~-[(6R)-6,8-DISULFANYLOCTANOYL]-L-LYSINE'>LA2</scene></td></tr>
-{{STRUCTURE_3a8j|  PDB=3a8j  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3a8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a8j OCA], [https://pdbe.org/3a8j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a8j RCSB], [https://www.ebi.ac.uk/pdbsum/3a8j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a8j ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/3a8j_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=3a8j ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Aminomethyltransferase, a component of the glycine cleavage system termed T-protein, reversibly catalyzes the degradation of the aminomethyl moiety of glycine attached to the lipoate cofactor of H-protein, resulting in the production of ammonia, 5,10-methylenetetrahydrofolate, and dihydrolipoate-bearing H-protein in the presence of tetrahydrofolate. Several mutations in the human T-protein gene are known to cause nonketotic hyperglycinemia. Here, we report the crystal structure of Escherichia coli T-protein in complex with dihydrolipoate-bearing H-protein and 5-methyltetrahydrofolate, a complex mimicking the ternary complex in the reverse reaction. The structure of the complex shows a highly interacting intermolecular interface limited to a small area and the protein-bound dihydrolipoyllysine arm inserted into the active site cavity of the T-protein. Invariant Arg(292) of the T-protein is essential for complex assembly. The structure also provides novel insights in understanding the disease-causing mutations, in addition to the disease-related impairment in the cofactor-enzyme interactions reported previously. Furthermore, structural and mutational analyses suggest that the reversible transfer of the methylene group between the lipoate and tetrahydrofolate should proceed through the electron relay-assisted iminium intermediate formation.
-===Crystal Structure of ET-EHred complex===
+Crystal structure of aminomethyltransferase in complex with dihydrolipoyl-H-protein of the glycine cleavage system: implications for recognition of lipoyl protein substrate, disease-related mutations, and reaction mechanism.,Okamura-Ikeda K, Hosaka H, Maita N, Fujiwara K, Yoshizawa AC, Nakagawa A, Taniguchi H J Biol Chem. 2010 Jun 11;285(24):18684-92. Epub 2010 Apr 6. PMID:20375021<ref>PMID:20375021</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3a8j" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-A8J is a 6 chains structure with sequences 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=3A8J OCA].
+*[[Aminomethyltransferase 3D structures|Aminomethyltransferase 3D structures]]
-[[Category: Aminomethyltransferase]]
+== References ==
-[[Category: Escherichia coli]]
+<references/>
-[[Category: Hosaka, H.]]
+__TOC__
-[[Category: Okamura-Ikeda, K.]]
+</StructureSection>
-[[Category: Aminotransferase]]
+[[Category: Escherichia coli K-12]]
-[[Category: Glycine cleavage system]]
+[[Category: Large Structures]]
-[[Category: Lipoyl]]
+[[Category: Hosaka H]]
-[[Category: Transferase]]
+[[Category: Okamura-Ikeda K]]
-[[Category: Transferase-transport protein complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr  7 10:45:10 2010''