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1gjx

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{{STRUCTURE_1gjx| PDB=1gjx | SCENE= }}
{{STRUCTURE_1gjx| PDB=1gjx | SCENE= }}
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'''SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE CHIMERIC DIHYDROLIPOYL DEHYDROGENASE P64K FROM NEISSERIA MENINGITIDIS'''
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===SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE CHIMERIC DIHYDROLIPOYL DEHYDROGENASE P64K FROM NEISSERIA MENINGITIDIS===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11559360 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11559360}}
==About this Structure==
==About this Structure==
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1GJX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA].
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1GJX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA].
==Reference==
==Reference==
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[[Category: Neisseria meningitidi]]
[[Category: Neisseria meningitidi]]
[[Category: Post-translational modification]]
[[Category: Post-translational modification]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:24:40 2008''

Revision as of 02:24, 1 July 2008

Image:1gjx.png

Template:STRUCTURE 1gjx

SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE CHIMERIC DIHYDROLIPOYL DEHYDROGENASE P64K FROM NEISSERIA MENINGITIDIS

Template:ABSTRACT PUBMED 11559360

About this Structure

1GJX is a Single protein structure of sequence from Neisseria meningitidis. Full experimental information is available from OCA.

Reference

Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis., Tozawa K, Broadhurst RW, Raine AR, Fuller C, Alvarez A, Guillen G, Padron G, Perham RN, Eur J Biochem. 2001 Sep;268(18):4908-17. PMID:11559360

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