2kb4: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{STRUCTURE_2kb4|  PDB=2kb4  |  SCENE=  }}
-===NMR structure of the unphosphorylated form of OdhI, OdhI.===
-{{ABSTRACT_PUBMED_19368890}}
-==Function==
+==NMR structure of the unphosphorylated form of OdhI, OdhI.==
-[[http://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.
+<StructureSection load='2kb4' size='340' side='right'caption='[[2kb4]]' scene=''>
+== 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.
-==About this Structure==
+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>
-[[2kb4]] is a 1 chain structure with sequence from [http://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].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<ref group="xtra">PMID:019368890</ref><references group="xtra"/><references/>
+</div>
+<div class="pdbe-citations 2kb4" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Corynebacterium glutamicum]]
-[[Category: Barthe, P.]]
+[[Category: Large Structures]]
-[[Category: Canova, M.]]
+[[Category: Barthe P]]
-[[Category: Cohen-Gonsaud, M.]]
+[[Category: Canova M]]
-[[Category: Hurard, C.]]
+[[Category: Cohen-Gonsaud M]]
-[[Category: Molle, V.]]
+[[Category: Hurard C]]
-[[Category: Roumestand, C.]]
+[[Category: Molle V]]
-[[Category: Dehydrogenase inhibitor]]
+[[Category: Roumestand C]]
-[[Category: Fha]]
-[[Category: Forkhead-associated domain]]
-[[Category: Gara]]
-[[Category: Kinase substrate]]
-[[Category: Phosphoprotein]]