1u22: Difference between revisions

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-[[Image:1u22.png|left|200px]]
-{{STRUCTURE_1u22|  PDB=1u22  |  SCENE=  }}
+==A. thaliana cobalamine independent methionine synthase==
+<StructureSection load='1u22' size='340' side='right'caption='[[1u22]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1u22]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U22 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1u22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u22 OCA], [https://pdbe.org/1u22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u22 RCSB], [https://www.ebi.ac.uk/pdbsum/1u22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u22 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/METE1_ARATH METE1_ARATH] Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.<ref>PMID:15024005</ref>
+== 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/u2/1u22_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1u22 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Cobalamin-independent methionine synthase (MetE) catalyzes the synthesis of methionine by a direct transfer of the methyl group of N5-methyltetrahydrofolate (CH3-H2PteGlun) to the sulfur atom of homocysteine (Hcy). We report here the first crystal structure of this metalloenzyme under different forms, free or complexed with the Hcy and folate substrates. The Arabidopsis thaliana MetE (AtMetE) crystals reveal a monomeric structure built by two (betaalpha)8 barrels making a deep groove at their interface. The active site is located at the surface of the C-terminal domain, facing the large interdomain cleft. Inside the active site, His647, Cys649, and Cys733 are involved in zinc coordination, whereas Asp605, Ile437, and Ser439 interact with Hcy. Opposite the zinc/Hcy binding site, a cationic loop (residues 507-529) belonging to the C-terminal domain anchors the first glutamyl residue of CH3-H4PteGlu5. The pterin moiety of CH3-H4PteGlu5 is stacked with Trp567, enabling the N5-methyl group to protrude in the direction of the zinc atom. These data suggest a structural role of the N-terminal domain of AtMetE in the stabilization of loop 507-529 and in the interaction with the poly-glutamate chain of CH3-H4PteGlun. Comparison of AtMetE structures reveals that the addition of Hcy does not lead to a direct coordination of the sulfur atom with zinc but to a reorganization of the zinc binding site with a stronger coordination to Cys649, Cys733, and a water molecule.
-===A. thaliana cobalamine independent methionine synthase===
+Crystal structures of cobalamin-independent methionine synthase complexed with zinc, homocysteine, and methyltetrahydrofolate.,Ferrer JL, Ravanel S, Robert M, Dumas R J Biol Chem. 2004 Oct 22;279(43):44235-8. Epub 2004 Aug 23. PMID:15326182<ref>PMID:15326182</ref>
-{{ABSTRACT_PUBMED_15326182}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1u22" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-[[1u22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U22 OCA].
+*[[Methionine synthase 3D structures|Methionine synthase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:015326182</ref><references group="xtra"/>
+__TOC__
-[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
+</StructureSection>
 [[Category: Arabidopsis thaliana]]
-[[Category: Dumas, R.]]
+[[Category: Large Structures]]
-[[Category: Ferrer, J L.]]
+[[Category: Dumas R]]
-[[Category: Ravanel, S.]]
+[[Category: Ferrer J-L]]
-[[Category: Robert, M.]]
+[[Category: Ravanel S]]
-[[Category: Homocysteine]]
+[[Category: Robert M]]
-[[Category: Methionine]]
-[[Category: Methyltetrahydrofolate]]
-[[Category: Synthase]]
-[[Category: Transferase]]