2kb3
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2kb3 is ON HOLD Authors: Barthe, P.PB., Roumestand, C.CR., Canova, M.MC., Hurard, C.CH., Molle, V.VM., Cohen-Gonsaud, M.MCG. Description: NMR Struc...) |
|||
| (13 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==NMR Structure of the phosphorylated form of OdhI, pOdhI.== | |
| + | <StructureSection load='2kb3' size='340' side='right'caption='[[2kb3]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2kb3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KB3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 30 models</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=2kb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kb3 OCA], [https://pdbe.org/2kb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kb3 RCSB], [https://www.ebi.ac.uk/pdbsum/2kb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kb3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ODHI_CORGL ODHI_CORGL] An essential component of the PknG signaling pathway. When unphosphorylated, it inhibits the activity of 2-oxoglutarate dehydrogenase. When phosphorylated it does not inhibit 2-oxoglutarate dehydrogenase. | ||
| + | == 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/kb/2kb3_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=2kb3 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The OdhI protein is key regulator of the TCA cycle in Corynebacterium glutamicum. This highly conserved protein is found in GC rich Gram-positive bacteria (e.g., the pathogenic Mycobacterium tuberculosis). The unphosphorylated form of OdhI inhibits the OdhA protein, a key enzyme of the TCA cycle, whereas the phosphorylated form is inactive. OdhI is predicted to be mainly a single FHA domain, a module that mediates protein-protein interaction through binding of phosphothreonine peptides, with a disordered N-terminal extension substrate of the serine/threonine protein kinases. In this study, we solved the solution structure of the unphosphorylated and phosphorylated isoforms of the protein. We observed a major conformational change between the two forms characterized by the binding of the phosphorylated N-terminal part of the protein to its own FHA domain, consequently inhibiting it. This structural observation corresponds to a new autoinhibition mechanism described for a FHA domain protein. | ||
| - | + | Dynamic and structural characterization of a bacterial FHA protein reveals a new autoinhibition mechanism.,Barthe P, Roumestand C, Canova MJ, Kremer L, Hurard C, Molle V, Cohen-Gonsaud M Structure. 2009 Apr 15;17(4):568-78. PMID:19368890<ref>PMID:19368890</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2kb3" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Corynebacterium glutamicum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Barthe P]] | ||
| + | [[Category: Canova M]] | ||
| + | [[Category: Cohen-Gonsaud M]] | ||
| + | [[Category: Hurard C]] | ||
| + | [[Category: Molle V]] | ||
| + | [[Category: Roumestand C]] | ||
Current revision
NMR Structure of the phosphorylated form of OdhI, pOdhI.
| |||||||||||
