PDBsum entry 1m3e

Transferase

PDB id

1m3e

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Contents

			Protein chains

					472 a.a. *

			Waters ×859

* Residue conservation analysis

PDB id:

1m3e

Links

Name:

Transferase

Title:

Succinyl-coa:3-ketoacid coa transferase from pig heart (selenomethionine)

Structure:

Succinyl-coa:3-ketoacid-coenzyme a transferase. Chain: a, b, c, d. Synonym: succinyl coa:3-oxoacid coa-transferase. Engineered: yes

Source:

Sus scrofa. Pig. Organism_taxid: 9823. Organ: heart. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

2.50Å

R-factor:

0.221

R-free:

0.265

Authors:

K.S.Bateman,E.R.Brownie,W.T.Wolodko,M.E.Fraser

Key ref:

K.S.Bateman et al. (2002). Structure of the mammalian CoA transferase from pig heart. Biochemistry, 41, 14455-14462. PubMed id: 12463743 DOI: 10.1021/bi020568f

Date:

27-Jun-02

Release date:

07-Jan-03

PROCHECK

	Headers

	References

Protein chains

Q29551 (SCOT1_PIG) - Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial from Sus scrofa

Seq: Struc:

Seq: Struc:					520 a.a. 472 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)



		Enzyme reactions

Enzyme class:

E.C.2.8.3.5 - 3-oxoacid CoA-transferase.

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

Reaction:

a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-CoA + succinate

3-oxo acid	+	succinyl-CoA	=	3-oxoacyl-CoA	+	succinate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1021/bi020568f	Biochemistry 41:14455-14462 (2002)
PubMed id: 12463743

Structure of the mammalian CoA transferase from pig heart.
K.S.Bateman, E.R.Brownie, W.T.Wolodko, M.E.Fraser.

ABSTRACT

Ketoacidosis affects patients who are deficient in the enzyme activity of succinyl-CoA:3-ketoacid CoA transferase (SCOT), since SCOT catalyses the activation of acetoacetate in the metabolism of ketone bodies. Thus far, structure/function analysis of the mammalian enzyme has been predicted based on the three-dimensional structure of a CoA transferase determined from an anaerobic bacterium that utilizes its enzyme for glutamate fermentation. To better interpret clinical data, we have determined the structure of a mammalian CoA transferase from pig heart by X-ray crystallography to 2.5 A resolution. Instrumental to the structure determination were selenomethionine substitution and the use of argon during purification and crystallization. Although pig heart SCOT adopts an alpha/beta protein fold, resembling the overall fold of the bacterial CoA transferase, several loops near the active site of pig heart SCOT follow different paths than the corresponding loops in the bacterial enzyme, accounting for differences in substrate specificities. Two missense mutations found associated with SCOT of ketoacidosis patients were mapped to a location in the structure that might disrupt the stabilization of the amino-terminal strand and thereby interfere with the proper folding of the protein into a functional enzyme.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21253865

Y.Wang, H.Sun, Y.Ru, S.Yin, L.Yin, and S.Liu (2011).
Proteomic survey towards the tissue-specific proteins of mouse mitochondria.

Sci China Life Sci, 54, 3.

20606260

S.F.Coker, A.J.Lloyd, E.Mitchell, G.R.Lewis, A.R.Coker, and P.M.Shoolingin-Jordan (2010).
The high-resolution structure of pig heart succinyl-CoA:3-oxoacid coenzyme A transferase.

Acta Crystallogr D Biol Crystallogr, 66, 797-805.

PDB code:

3k6m

19804364

S.Macieira, J.Zhang, M.Velarde, W.Buckel, and A.Messerschmidt (2009).
Crystal structure of 4-hydroxybutyrate CoA-transferase from Clostridium aminobutyricum.

Biol Chem, 390, 1251-1263.

PDB code:

3gk7

17685555

I.Rebrin, C.Brégère, S.Kamzalov, T.K.Gallaher, and R.S.Sohal (2007).
Nitration of tryptophan 372 in succinyl-CoA:3-ketoacid CoA transferase during aging in rat heart mitochondria.

Biochemistry, 46, 10130-10144.

16253988

E.S.Rangarajan, Y.Li, E.Ajamian, P.Iannuzzi, S.D.Kernaghan, M.E.Fraser, M.Cygler, and A.Matte (2005).
Crystallographic trapping of the glutamyl-CoA thioester intermediate of family I CoA transferases.

J Biol Chem, 280, 42919-42928.

PDB codes:

2ahu 2ahv 2ahw

15388917

A.M.Coros, L.Swenson, W.T.Wolodko, and M.E.Fraser (2004).
Structure of the CoA transferase from pig heart to 1.7 A resolution.

Acta Crystallogr D Biol Crystallogr, 60, 1717-1725.

PDB codes:

1ooy 1ooz 1ope

15326192

L.Rivière, S.W.van Weelden, P.Glass, P.Vegh, V.Coustou, M.Biran, J.J.van Hellemond, F.Bringaud, A.G.Tielens, and M.Boshart (2004).
Acetyl:succinate CoA-transferase in procyclic Trypanosoma brucei. Gene identification and role in carbohydrate metabolism.

J Biol Chem, 279, 45337-45346.

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. Where a reference describes a PDB structure, the PDB code is shown on the right.