This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1x2g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1x2g.gif|left|200px]]
[[Image:1x2g.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1x2g |SIZE=350|CAPTION= <scene name='initialview01'>1x2g</scene>, resolution 2.40&Aring;
+
The line below this paragraph, containing "STRUCTURE_1x2g", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1x2g| PDB=1x2g | SCENE= }}
-
|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>
+
-
}}
+
'''Crystal Structure of Lipate-Protein Ligase A from Escherichia coli'''
'''Crystal Structure of Lipate-Protein Ligase A from Escherichia coli'''
Line 31: Line 28:
[[Category: Taniguchi, H.]]
[[Category: Taniguchi, H.]]
[[Category: Toma, S.]]
[[Category: Toma, S.]]
-
[[Category: lipoate-protein ligase]]
+
[[Category: Lipoate-protein ligase]]
-
[[Category: lipoic acid]]
+
[[Category: Lipoic acid]]
-
[[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 14:26:32 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:43:58 2008''
+

Revision as of 11:26, 3 May 2008

Template:STRUCTURE 1x2g

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 Sat May 3 14:26:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools