1x2g
From Proteopedia
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|PDB= 1x2g |SIZE=350|CAPTION= <scene name='initialview01'>1x2g</scene>, resolution 2.40Å | |PDB= 1x2g |SIZE=350|CAPTION= <scene name='initialview01'>1x2g</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1x2h|1X2H]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x2g OCA], [http://www.ebi.ac.uk/pdbsum/1x2g PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1x2g RCSB]</span> | ||
}} | }} | ||
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[[Category: protein acylation]] | [[Category: protein acylation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:43:58 2008'' |
Revision as of 21:43, 30 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1X2H
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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