1GJX

Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis

Summary for 1GJX

• Entry DOI: 10.2210/pdb1gjx/pdb
• Descriptor: PYRUVATE DEHYDROGENASE (1 entity in total)
• Functional Keywords: oxidoreductase, lipoyl domain, dihydrolipoyl dehydrogenase, multienzyme complex, neisseria meningitidis, post-translational modification
• Biological source: NEISSERIA MENINGITIDIS
• Total number of polymer chains: 1
• Total formula weight: 8329.45

Authors

Tozawa, K.,Broadhurst, R.W.,Raine, A.R.C.,Fuller, C.,Alvarez, A.,Guillen, G.,Padron, G.,Perham, R.N. (deposition date: 2001-08-03, release date: 2001-11-28, Last modification date: 2024-05-15)

Primary citation

Tozawa, K.,Broadhurst, R.W.,Raine, A.R.,Fuller, C.,Alvarez, A.,Guillen, G.,Padron, G.,Perham, R.N.
Solution Structure of the Lipoyl Domain of the Chimeric Dihydrolipoyl Dehydrogenase P64K from Neisseria Meningitidis
Eur.J.Biochem., 268:4908-, 2001

PubMed Abstract: The antigenic P64K protein from the pathogenic bacterium Neisseria meningitidis is found in the outer membrane of the cell, and consists of two parts: an 81-residue N-terminal region and a 482-residue C-terminal region. The amino-acid sequence of the N-terminal region is homologous with the lipoyl domains of the dihydrolipoyl acyltransferase (E2) components, and that of the C-terminal region with the dihydrolipoyl dehydrogenase (E3) components, of 2-oxo acid dehydrogenase multienzyme complexes. The two parts are separated by a long linker region, similar to the linker regions in the E2 chains of 2-oxo acid dehydrogenase complexes, and it is likely this region is conformationally flexible. A subgene encoding the P64K lipoyl domain was created and over-expressed in Escherichia coli. The product was capable of post-translational modification by the lipoate protein ligase but not aberrant modification by the biotin protein ligase of E. coli. The solution structure of the apo-domain was determined by means of heteronuclear NMR spectroscopy and found to be a flattened beta barrel composed of two four-stranded antiparallel beta sheets. The lysine residue that becomes lipoylated is in an exposed beta turn that, from a [1H]-15N heteronuclear Overhauser effect experiment, appears to enjoy substantial local motion. This structure of a lipoyl domain derived from a dihydrolipoyl dehydrogenase resembles that of lipoyl domains normally found as part of the dihydrolipoyl acyltransferase component of 2-oxo acid dehydrogenase complexes and will assist in furthering the understanding of its function in a multienzyme complex and in the membrane-bound P64K protein itself.

PubMed: 11559360
DOI: 10.1046/J.0014-2956.2001.02422.X

Experimental method

SOLUTION NMR