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      <comment>Department of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, Budapest, 1094, Hungary            
            Department of Chemistry, Rutgers University, Newark, NJ 07102, United States            
            Cited By :5            
            Export Date: 15 January 2025            
            Correspondence Address: Ambrus, A.; Department of Biochemistry, Hungary; email: ambrus.attila@med.semmelweis-univ.hu            
            Correspondence Address: Jordan, F.; Department of Chemistry, United States; email: frjordan@newark.rutgers.edu</comment>
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      <title>Probing the E1o-E2o and E1a-E2o Interactions in Binary Subcomplexes of the Human 2-Oxoglutarate Dehydrogenase and 2-Oxoadipate Dehydrogenase Complexes by Chemical Cross-Linking Mass Spectrometry and Molecular Dynamics Simulation</title>
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      <abstractText>The human 2-oxoglutarate dehydrogenase complex (hOGDHc) is a key enzyme in the tricarboxylic acid cycle and is one of the main regulators of mitochondrial metabolism through NADH and reactive oxygen species levels. Evidence was obtained for formation of a hybrid complex between the hOGDHc and its homologue the 2-oxoadipate dehydrogenase complex (hOADHc) in the L-lysine metabolic pathway, suggesting a crosstalk between the two distinct pathways. Findings raised fundamental questions about the assembly of hE1a (2-oxoadipate-dependent E1 component) and hE1o (2-oxoglutarate-dependent E1) to the common hE2o core component. Here we report chemical cross-linking mass spectrometry (CL-MS) and molecular dynamics (MD) simulation analyses to understand assembly in binary subcomplexes. The CL-MS studies revealed the most prominent loci for hE1o-hE2o and hE1a-hE2o interactions and suggested different binding modes. The MD simulation studies led to the following conclusions: (i) The N-terminal regions in E1s are shielded by, but do not interact directly with hE2o. (ii) The hE2o linker region exhibits the highest number of H-bonds with the N-terminus and α/β1 helix of hE1o, yet with the interdomain linker and α/β1 helix of hE1a. (iii) The C-termini are involved in dynamic interactions in complexes, suggesting the presence of at least two conformations in solution.</abstractText>
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				&lt;div class=&quot;journal-subject&quot;&gt;Folyóirat szakterülete: Scopus - Catalysis&amp;nbsp;&amp;nbsp;&amp;nbsp;SJR indikátor:&amp;nbsp;Q2&lt;/div&gt;
				&lt;div class=&quot;journal-subject&quot;&gt;Folyóirat szakterülete: Scopus - Molecular Biology&amp;nbsp;&amp;nbsp;&amp;nbsp;SJR indikátor:&amp;nbsp;Q2&lt;/div&gt;
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		| Független: 6
		| Függő: 1
		| Nem jelölt: 0
		| WoS jelölt: 6 
		|  Scopus jelölt:&amp;nbsp;7 
		|  WoS/Scopus jelölt:&amp;nbsp;7 
		|  DOI jelölt:&amp;nbsp;7 
		
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    | &lt;span class=&quot;status-data status-ADMIN_APPROVED&quot;&gt; 	Admin láttamozott
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    | &lt;span class=&quot;type-subtype&quot;&gt;Folyóiratcikk
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      		| &lt;span class=&quot;pub-category&quot;&gt;Tudományos&lt;/span&gt;
	| &lt;span class=&quot;publication-sourceOfData&quot;&gt;Bibtex&lt;/span&gt;
&lt;/div&gt;

&lt;div class=&quot;funder&quot;&gt; (TKP2021-EGA-25),    Hungarian National Brain Research Program(2017-1.2.1-NKP-2017-00002),    (STIA-OTKA-2021),    OTKA(143627)   &lt;/div&gt;
&lt;div class=&quot;lastModified&quot;&gt;Utolsó módosítás: 2026.04.20. 11:38 Kajtár Virág Anna (SE_AOK_Biokemia_Admin5_KV, admin)
&lt;/div&gt;




	&lt;pre class=&quot;comment&quot; style=&quot;margin-top: 0; margin-bottom: 0;&quot;&gt;&lt;u&gt;Megjegyzés&lt;/u&gt;: Department of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, Budapest, 1094, Hungary            
            Department of Chemistry, Rutgers University, Newark, NJ 07102, United States            
            Cited By :5            
            Export Date: 15 January 2025            
            Correspondence Address: Ambrus, A.; Department of Biochemis...&lt;/pre&gt;

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