PDBsum entry 3a7u

Transferase

PDB id

3a7u

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Contents

			Protein chain

					325 a.a. *

* Residue conservation analysis

PDB id:

3a7u

Links

Name:

Transferase

Title:

Crystal structure of the bovine lipoyltransferase in its unliganded form

Structure:

Lipoyltransferase 1, mitochondrial. Chain: a. Fragment: unp residues 27-373. Synonym: lipoate-protein ligase, lipoate biosynthesis protein, lipoyl ligase. Engineered: yes

Source:

Bos taurus. Bovine. Organism_taxid: 9913. Gene: lipt1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

3.44Å

R-factor:

0.248

R-free:

0.318

Authors:

K.Fujiwara,H.Hosaka,A.Nakagawa

Key ref:

K.Fujiwara et al. (2010). Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A. J Biol Chem, 285, 9971-9980. PubMed id: 20089862 DOI: 10.1074/jbc.M109.078717

Date:

05-Oct-09

Release date:

19-Jan-10

PROCHECK

	Headers

	References

Protein chain

O46419 (LIPT_BOVIN) - Lipoyltransferase 1, mitochondrial from Bos taurus

Seq: Struc:					373 a.a. 325 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.2.3.1.- - ?????

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1074/jbc.M109.078717	J Biol Chem 285:9971-9980 (2010)
PubMed id: 20089862

Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A.
K.Fujiwara, N.Maita, H.Hosaka, K.Okamura-Ikeda, A.Nakagawa, H.Taniguchi.

ABSTRACT

Lipoate-protein ligase A (LplA) catalyzes the attachment of lipoic acid to lipoate-dependent enzymes by a two-step reaction: first the lipoate adenylation reaction and, second, the lipoate transfer reaction. We previously determined the crystal structure of Escherichia coli LplA in its unliganded form and a binary complex with lipoic acid (Fujiwara, K., Toma, S., Okamura-Ikeda, K., Motokawa, Y., Nakagawa, A., and Taniguchi, H. (2005) J Biol. Chem. 280, 33645-33651). Here, we report two new LplA structures, LplA.lipoyl-5'-AMP and LplA.octyl-5'-AMP.apoH-protein complexes, which represent the post-lipoate adenylation intermediate state and the pre-lipoate transfer intermediate state, respectively. These structures demonstrate three large scale conformational changes upon completion of the lipoate adenylation reaction: movements of the adenylate-binding and lipoate-binding loops to maintain the lipoyl-5'-AMP reaction intermediate and rotation of the C-terminal domain by about 180 degrees . These changes are prerequisites for LplA to accommodate apoprotein for the second reaction. The Lys(133) residue plays essential roles in both lipoate adenylation and lipoate transfer reactions. Based on structural and kinetic data, we propose a reaction mechanism driven by conformational changes.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21338421

Q.H.Christensen, N.Martin, M.C.Mansilla, D.de Mendoza, and J.E.Cronan (2011).
A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis.

Mol Microbiol, 80, 350-363.

20534555

C.Uttamapinant, K.A.White, H.Baruah, S.Thompson, M.Fernández-Suárez, S.Puthenveetil, and A.Y.Ting (2010).
A fluorophore ligase for site-specific protein labeling inside living cells.

Proc Natl Acad Sci U S A, 107, 10914-10919.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.