2kb4
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:2kb4.jpg|left|200px]] | ||
- | < | + | ==NMR structure of the unphosphorylated form of OdhI, OdhI.== |
- | + | <StructureSection load='2kb4' size='340' side='right'caption='[[2kb4]]' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[2kb4]] 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=2KB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KB4 FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2kb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kb4 OCA], [https://pdbe.org/2kb4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kb4 RCSB], [https://www.ebi.ac.uk/pdbsum/2kb4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kb4 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/2kb4_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=2kb4 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 2kb4" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | |
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- | == | + | |
- | < | + | |
[[Category: Corynebacterium glutamicum]] | [[Category: Corynebacterium glutamicum]] | ||
- | [[Category: Barthe | + | [[Category: Large Structures]] |
- | [[Category: Canova | + | [[Category: Barthe P]] |
- | [[Category: Cohen-Gonsaud | + | [[Category: Canova M]] |
- | [[Category: Hurard | + | [[Category: Cohen-Gonsaud M]] |
- | [[Category: Molle | + | [[Category: Hurard C]] |
- | [[Category: Roumestand | + | [[Category: Molle V]] |
- | + | [[Category: Roumestand C]] | |
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Current revision
NMR structure of the unphosphorylated form of OdhI, OdhI.
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