3flm: Difference between revisions

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-[[Image:3flm.png|left|200px]]
-{{STRUCTURE_3flm|  PDB=3flm  |  SCENE=  }}
+==Crystal structure of menD from E.coli==
+<StructureSection load='3flm' size='340' side='right'caption='[[3flm]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3flm]] is a 2 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=3FLM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FLM 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]] 2.7&#8491;</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=3flm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3flm OCA], [https://pdbe.org/3flm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3flm RCSB], [https://www.ebi.ac.uk/pdbsum/3flm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3flm ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MEND_ECOLI MEND_ECOLI] Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).<ref>PMID:1459959</ref> <ref>PMID:17760421</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/fl/3flm_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=3flm ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+MenD (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate) synthase belongs to the superfamily of thiamin diphosphate-dependent decarboxylases, which converts isochorismate and 2-oxoglutarate to SHCHC, pyruvate, and carbon dioxide. Here, we report the first crystal structure of apo-MenD from Escherichia coli determined in tetragonal crystal form. The subunit displays the typical three-domain structure observed for ThDP-dependent enzymes. Analytical gel filtration shows that EcMenD behaves as a dimer as well as a tetramer. Circular dichroism and isothermal calorimetry results confirm EcMenD dependency on ThDP, which concomitantly helps to stabilize with better configuration.
-===Crystal structure of menD from E.coli===
+Structural insights of the MenD from Escherichia coli reveal ThDP affinity.,Priyadarshi A, Saleem Y, Nam KH, Kim KS, Park SY, Kim EE, Hwang KY Biochem Biophys Res Commun. 2009 Mar 20;380(4):797-801. Epub 2009 Feb 4. PMID:19338755<ref>PMID:19338755</ref>
-{{ABSTRACT_PUBMED_19338755}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 3flm" style="background-color:#fffaf0;"></div>
-[[3flm]] is a 2 chain structure of [[Mitogen-activated protein kinase]] with sequence from [http://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=3FLM OCA].
 ==See Also==
-*[[Mitogen-activated protein kinase|Mitogen-activated protein kinase]]
+*[[Mitogen-activated protein kinase 3D structures|Mitogen-activated protein kinase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:019338755</ref><references group="xtra"/>
+__TOC__
-[[Category: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase]]
+</StructureSection>
-[[Category: Escherichia coli k-12]]
+[[Category: Escherichia coli K-12]]
-[[Category: Hwang, K Y.]]
+[[Category: Large Structures]]
-[[Category: Priyadarshi, A.]]
+[[Category: Hwang KY]]
-[[Category: Magnesium]]
+[[Category: Priyadarshi A]]
-[[Category: Manganese]]
-[[Category: Menaquinone biosynthesis]]
-[[Category: Menaquinone biosynthesis protein]]
-[[Category: Metal-binding]]
-[[Category: Thiamine pyrophosphate]]
-[[Category: Transferase]]