1x2h: Difference between revisions

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[[Image:1x2h.gif|left|200px]]<br /><applet load="1x2h" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1x2h.gif|left|200px]]<br /><applet load="1x2h" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1x2h, resolution 2.91Å" />

'''Crystal Structure of Lipate-Protein Ligase A from Escherichia coli complexed with lipoic acid'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with LPA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1X2H OCA].

1X2H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=LPA:'>LPA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X2H OCA].

==Reference==

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[[Category: protein acylation]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 05:48:~~34 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:50:23 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1x2h.gif|left|200px]]<br /><applet load="1x2h" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1x2h.gif|left|200px]]<br /><applet load="1x2h" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1x2h, resolution 2.91&Aring;" />
 '''Crystal Structure of Lipate-Protein Ligase A from Escherichia coli complexed with lipoic acid'''<br />
 ==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.
+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==
-X2H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with LPA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1X2H OCA].
+X2H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=LPA:'>LPA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X2H OCA].
 ==Reference==
@@ Line 25: / Line 25: @@
 [[Category: protein acylation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:48:34 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:50:23 2008''