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2kb3

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Revision as of 10:36, 18 July 2018

NMR Structure of the phosphorylated form of OdhI, pOdhI.

Structural highlights

2kb3 is a 1 chain structure with sequence from "micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	2kb4
Gene:	cg1630, Cgl1441, odhI ("Micrococcus glutamicus" Kinoshita et al. 1958)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Barthe P, Roumestand C, Canova MJ, Kremer L, Hurard C, Molle V, Cohen-Gonsaud M. Dynamic and structural characterization of a bacterial FHA protein reveals a new autoinhibition mechanism. Structure. 2009 Apr 15;17(4):568-78. PMID:19368890 doi:10.1016/j.str.2009.02.012

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2kb3"

@@ Line 1: / Line 1: @@
 ==NMR Structure of the phosphorylated form of OdhI, pOdhI.==
 <StructureSection load='2kb3' size='340' side='right' caption='[[2kb3]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kb4|2kb4]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cg1630, Cgl1441, odhI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 "Micrococcus glutamicus" Kinoshita et al. 1958])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kb3 OCA], [http://pdbe.org/2kb3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kb3 RCSB], [http://www.ebi.ac.uk/pdbsum/2kb3 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kb3 OCA], [http://pdbe.org/2kb3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kb3 RCSB], [http://www.ebi.ac.uk/pdbsum/2kb3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kb3 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kb/2kb3_consurf.spt"</scriptWhenChecked>
+    <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/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 40: / Line 41: @@
 [[Category: Molle, V]]
 [[Category: Roumestand, C]]
+[[Category: Cytoplasm]]
 [[Category: Dehydrogenase inhibitor]]
 [[Category: Fha]]

2kb3

From Proteopedia

Revision as of 10:36, 18 July 2018

NMR Structure of the phosphorylated form of OdhI, pOdhI.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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