1x2g
From Proteopedia
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| - | [[Image:1x2g.gif|left|200px]] | + | [[Image:1x2g.gif|left|200px]] |
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| - | '''Crystal Structure of Lipate-Protein Ligase A from Escherichia coli''' | + | {{Structure |
| + | |PDB= 1x2g |SIZE=350|CAPTION= <scene name='initialview01'>1x2g</scene>, resolution 2.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal Structure of Lipate-Protein Ligase A from Escherichia coli''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1X2G is a [ | + | 1X2G 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=1X2G 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 15:04:19 2008'' |
Revision as of 13:04, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Lipate-Protein Ligase A from Escherichia coli
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
1X2G 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
Page seeded by OCA on Thu Mar 20 15:04:19 2008
