We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2e5a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2e5a.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2e5a.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2e5a| PDB=2e5a | SCENE= }}
{{STRUCTURE_2e5a| PDB=2e5a | SCENE= }}
-
'''Crystal Structure of Bovine Lipoyltransferase in Complex with Lipoyl-AMP'''
+
===Crystal Structure of Bovine Lipoyltransferase in Complex with Lipoyl-AMP===
-
==Overview==
+
<!--
-
Lipoic acid is an essential cofactor of the alpha-ketoacid dehydrogenase complexes and the glycine cleavage system. It is covalently attached to a specific lysine residue of the subunit of the complexes. The bovine lipoyltransferase (bLT) catalyzes the lipoic acid attachment reaction using lipoyl-AMP as a substrate, forming a lipoylated protein and AMP. To gain insights into the reaction mechanism at the atomic level, we have determined the crystal structure of bLT at 2.10 A resolution. Unexpectedly, the purified recombinant bLT contains endogenous lipoyl-AMP. The structure of bLT consists of N-terminal and C-terminal domains, and lipoyl-AMP is bound to the active site in the N-terminal domain, adopting a U-shaped conformation. The lipoyl moiety is buried in the hydrophobic pocket, forming van der Waals interactions, and the AMP moiety forms numerous hydrogen bonds with bLT in another tunnel-like cavity. These interactions work together to expose the C10 atom of lipoyl-AMP to the surface of the bLT molecule. The carbonyl oxygen atom of lipoyl-AMP interacts with the invariant Lys135. The interaction might stimulate the positive charge of the C10 atom of lipoyl-AMP, and consequently facilitate the nucleophilic attack by the lysine residue of the lipoate-acceptor protein, accompanying the bond cleavage between the carbonyl group and the phosphate group. We discuss the structural differences between bLT and the lipoate-protein ligase A from Escherichia coli and Thermoplasma acidophilum. We further demonstrate that bLT in mitochondria also contains endogenous lipoylmononucleotide, being ready for the lipoylation of apoproteins.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17570395}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17570395 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17570395}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Lipoyl-amp]]
[[Category: Lipoyl-amp]]
[[Category: Lipoyltransferase]]
[[Category: Lipoyltransferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:56:26 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:06:47 2008''

Revision as of 21:06, 28 July 2008

Image:2e5a.png

Template:STRUCTURE 2e5a

Crystal Structure of Bovine Lipoyltransferase in Complex with Lipoyl-AMP

Template:ABSTRACT PUBMED 17570395

About this Structure

2E5A is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Crystal structure of bovine lipoyltransferase in complex with lipoyl-AMP., Fujiwara K, Hosaka H, Matsuda M, Okamura-Ikeda K, Motokawa Y, Suzuki M, Nakagawa A, Taniguchi H, J Mol Biol. 2007 Aug 3;371(1):222-34. Epub 2007 May 26. PMID:17570395

Page seeded by OCA on Tue Jul 29 00:06:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2e5a"
Personal tools