1gkx

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(New page: 200px<br /><applet load="1gkx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gkx, resolution 2.30&Aring;" /> '''BRANCHED-CHAIN ALPHA...)
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[[Image:1gkx.gif|left|200px]]<br /><applet load="1gkx" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gkx, resolution 2.30&Aring;" />
 
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'''BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE KINASE (BCK)'''<br />
 
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==Overview==
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==Branched-chain alpha-ketoacid dehydrogenase kinase (BCK)==
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Mitochondrial protein kinases (mPKs) are molecular switches that, down-regulate the oxidation of branched-chain alpha-ketoacids and, pyruvate. Elevated levels of these metabolites are implicated in disease, states such as insulin-resistant Type II diabetes, branched-chain, ketoaciduria, and primary lactic acidosis. We report a three-dimensional, structure of a member of the mPK family, rat branched-chain alpha-ketoacid, dehydrogenase kinase (BCK). BCK features a characteristic, nucleotide-binding domain and a four-helix bundle domain. These two, domains are reminiscent of modules found in protein histidine kinases, (PHKs), which are involved in two-component signal transduction systems., Unlike PHKs, BCK dimerizes through direct interaction of two opposing, nucleotide-binding domains. Nucleotide binding to BCK is uniquely mediated, by both potassium and magnesium. Binding of ATP induces disorder-order, transitions in a loop region at the nucleotide-binding site. These, structural changes lead to the formation of a quadruple aromatic stack in, the interface between the nucleotide-binding domain and the four-helix, bundle domain, where they induce a movement of the top portion of two, helices. Phosphotransfer induces further ordering of the loop region, effectively trapping the reaction product ADP, which explains product, inhibition in mPKs. The BCK structure is a prototype for all mPKs and will, provide a framework for structure-assisted inhibitor design for this, family of kinases.
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<StructureSection load='1gkx' size='340' side='right'caption='[[1gkx]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1gkx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GKX FirstGlance]. <br>
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1GKX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/[3-methyl-2-oxobutanoate_dehydrogenase_(acetyl-transferring)]_kinase [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.4 2.7.11.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GKX OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gkx OCA], [https://pdbe.org/1gkx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gkx RCSB], [https://www.ebi.ac.uk/pdbsum/1gkx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gkx ProSAT]</span></td></tr>
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Structure of rat BCKD kinase: nucleotide-induced domain communication in a mitochondrial protein kinase., Machius M, Chuang JL, Wynn RM, Tomchick DR, Chuang DT, Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11218-23. Epub 2001 Sep 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11562470 11562470]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BCKD_RAT BCKD_RAT] Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways. Key enzyme that regulate the activity state of the BCKD complex.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gk/1gkx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1gkx ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Chuang DT]]
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[[Category: [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase]]
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[[Category: Chuang JL]]
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[[Category: Chuang, D.T.]]
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[[Category: Machius M]]
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[[Category: Chuang, J.L.]]
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[[Category: Tomchick DR]]
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[[Category: Machius, M.]]
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[[Category: Wynn RM]]
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[[Category: Tomchick, D.R.]]
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[[Category: Wynn, R.M.]]
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[[Category: CL]]
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[[Category: mitochondrial protein kinase]]
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[[Category: potassium]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:07:43 2007''
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Current revision

Branched-chain alpha-ketoacid dehydrogenase kinase (BCK)

PDB ID 1gkx

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