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| | {{STRUCTURE_2e5a| PDB=2e5a | SCENE= }} | | {{STRUCTURE_2e5a| PDB=2e5a | SCENE= }} |
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| - | '''Crystal Structure of Bovine Lipoyltransferase in Complex with Lipoyl-AMP'''
| + | ===Crystal Structure of Bovine Lipoyltransferase in Complex with Lipoyl-AMP=== |
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| - | ==Overview==
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| - | Lipoic acid is an essential cofactor of the alpha-ketoacid dehydrogenase complexes and the glycine cleavage system. It is covalently attached to a specific lysine residue of the subunit of the complexes. The bovine lipoyltransferase (bLT) catalyzes the lipoic acid attachment reaction using lipoyl-AMP as a substrate, forming a lipoylated protein and AMP. To gain insights into the reaction mechanism at the atomic level, we have determined the crystal structure of bLT at 2.10 A resolution. Unexpectedly, the purified recombinant bLT contains endogenous lipoyl-AMP. The structure of bLT consists of N-terminal and C-terminal domains, and lipoyl-AMP is bound to the active site in the N-terminal domain, adopting a U-shaped conformation. The lipoyl moiety is buried in the hydrophobic pocket, forming van der Waals interactions, and the AMP moiety forms numerous hydrogen bonds with bLT in another tunnel-like cavity. These interactions work together to expose the C10 atom of lipoyl-AMP to the surface of the bLT molecule. The carbonyl oxygen atom of lipoyl-AMP interacts with the invariant Lys135. The interaction might stimulate the positive charge of the C10 atom of lipoyl-AMP, and consequently facilitate the nucleophilic attack by the lysine residue of the lipoate-acceptor protein, accompanying the bond cleavage between the carbonyl group and the phosphate group. We discuss the structural differences between bLT and the lipoate-protein ligase A from Escherichia coli and Thermoplasma acidophilum. We further demonstrate that bLT in mitochondria also contains endogenous lipoylmononucleotide, being ready for the lipoylation of apoproteins.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17570395}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17570395 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17570395}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Lipoyl-amp]] | | [[Category: Lipoyl-amp]] |
| | [[Category: Lipoyltransferase]] | | [[Category: Lipoyltransferase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:56:26 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:06:47 2008'' |
Revision as of 21:06, 28 July 2008
Template:STRUCTURE 2e5a
Crystal Structure of Bovine Lipoyltransferase in Complex with Lipoyl-AMP
Template:ABSTRACT PUBMED 17570395
About this Structure
2E5A is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Crystal structure of bovine lipoyltransferase in complex with lipoyl-AMP., Fujiwara K, Hosaka H, Matsuda M, Okamura-Ikeda K, Motokawa Y, Suzuki M, Nakagawa A, Taniguchi H, J Mol Biol. 2007 Aug 3;371(1):222-34. Epub 2007 May 26. PMID:17570395
Page seeded by OCA on Tue Jul 29 00:06:47 2008
