1K8M

Solution Structure of the Lipoic Acid-Bearing Domain of the E2 component of Human, Mitochondrial Branched-Chain alpha-Ketoacid Dehydrogenase

Summary for 1K8M

• Entry DOI: 10.2210/pdb1k8m/pdb
• Related: 1K8O
• NMR Information: BMRB: 5078
• Descriptor: E2 component of Branched-Chain alpha-Ketoacid Dehydrogenase (1 entity in total)
• Functional Keywords: lipoyl acid bearing, human bckd, experimental nmr data, average structure, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion matrix: P11182
• Total number of polymer chains: 1
• Total formula weight: 10662.94

Authors

Chang, C.-F.,Chou, H.-T.,Chuang, J.L.,Chuang, D.T.,Huang, T.-h. (deposition date: 2001-10-24, release date: 2001-11-14, Last modification date: 2024-05-29)

Primary citation

Chang, C.-F.,Chou, H.-T.,Chuang, J.L.,Chuang, D.T.,Huang, T.-h.
Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex
J.Biol.Chem., 277:15865-15873, 2002

PubMed Abstract: The lipoyl-bearing domain (LBD) of the transacylase (E2) subunit of the branched-chain alpha-keto acid dehydrogenase complex plays a central role in substrate channeling in this mitochondrial multienzyme complex. We have employed multidimensional heteronuclear NMR techniques to determine the structure and dynamics of the LBD of the human branched-chain alpha-keto acid dehydrogenase complex (hbLBD). Similar to LBD from other members of the alpha-keto acid dehydrogenase family, the solution structure of hbLBD is a flattened beta-barrel formed by two four-stranded antiparallel beta-sheets. The lipoyl Lys(44) residue resides at the tip of a beta-hairpin comprising a sharp type I beta-turn and the two connecting beta-strands 4 and 5. A prominent V-shaped groove formed by a surface loop, L1, connecting beta 1- and beta 2-strands and the lipoyl lysine beta-hairpin constitutes the functional pocket. We further applied reduced spectral density functions formalism to extract dynamic information of hbLBD from (15)N-T(1), (15)N-T(2), and ((1)H-(15)N) nuclear Overhauser effect data obtained at 600 MHz. The results showed that residues surrounding the lipoyl lysine region comprising the L1 loop and the Lys(44) beta-turn are highly flexible, whereas beta-sheet S1 appears to display a slow conformational exchange process.

PubMed: 11839747
DOI: 10.1074/jbc.M110952200

Experimental method

SOLUTION NMR