1x2h: Difference between revisions
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'''Crystal Structure of Lipate-Protein Ligase A from Escherichia coli complexed with lipoic acid''' | {{Structure | ||
|PDB= 1x2h |SIZE=350|CAPTION= <scene name='initialview01'>1x2h</scene>, resolution 2.91Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=LPA:LIPOIC ACID'>LPA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal Structure of Lipate-Protein Ligase A from Escherichia coli complexed with lipoic acid''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1X2H is a [ | 1X2H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X2H OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site., Fujiwara K, Toma S, Okamura-Ikeda K, Motokawa Y, Nakagawa A, Taniguchi H, J Biol Chem. 2005 Sep 30;280(39):33645-51. Epub 2005 Jul 25. PMID:[http:// | Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site., Fujiwara K, Toma S, Okamura-Ikeda K, Motokawa Y, Nakagawa A, Taniguchi H, J Biol Chem. 2005 Sep 30;280(39):33645-51. Epub 2005 Jul 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16043486 16043486] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein acylation]] | [[Category: protein acylation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:04:20 2008'' | ||
Revision as of 13:04, 20 March 2008
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| 1x2h, resolution 2.91Å | |||||||||||||
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| Ligands: | LPA | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal Structure of Lipate-Protein Ligase A from Escherichia coli complexed with lipoic acid
Overview
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.
About this Structure
1X2H is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site., Fujiwara K, Toma S, Okamura-Ikeda K, Motokawa Y, Nakagawa A, Taniguchi H, J Biol Chem. 2005 Sep 30;280(39):33645-51. Epub 2005 Jul 25. PMID:16043486
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