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| {{STRUCTURE_1x2h| PDB=1x2h | SCENE= }} | | {{STRUCTURE_1x2h| PDB=1x2h | SCENE= }} |
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| '''Crystal Structure of Lipate-Protein Ligase A from Escherichia coli complexed with lipoic acid'''
| | ===Crystal Structure of Lipate-Protein Ligase A from Escherichia coli complexed with lipoic acid=== |
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| ==Overview==
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| Lipoate-protein ligase A (LplA) catalyzes the formation of lipoyl-AMP from lipoate and ATP and then transfers the lipoyl moiety to a specific lysine residue on the acyltransferase subunit of alpha-ketoacid dehydrogenase complexes and on H-protein of the glycine cleavage system. The lypoyllysine arm plays a pivotal role in the complexes by shuttling the reaction intermediate and reducing equivalents between the active sites of the components of the complexes. We have determined the X-ray crystal structures of Escherichia coli LplA alone and in a complex with lipoic acid at 2.4 and 2.9 angstroms resolution, respectively. The structure of LplA consists of a large N-terminal domain and a small C-terminal domain. The structure identifies the substrate binding pocket at the interface between the two domains. Lipoic acid is bound in a hydrophobic cavity in the N-terminal domain through hydrophobic interactions and a weak hydrogen bond between carboxyl group of lipoic acid and the Ser-72 or Arg-140 residue of LplA. No large conformational change was observed in the main chain structure upon the binding of lipoic acid.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16043486}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16043486 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16043486}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Post-translational modification]] | | [[Category: Post-translational modification]] |
| [[Category: Protein acylation]] | | [[Category: Protein acylation]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:26:35 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:02:49 2008'' |
