PDBsum entry 3pgm

Transferase (phosphoryl)

PDB id

3pgm

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Contents

			Protein chains

					230 a.a. *

			Ligands

					SO4 ×2


					SO4-3PG ×2

* Residue conservation analysis

PDB id:

3pgm

Links

Name:

Transferase (phosphoryl)

Title:

The structure of yeast phosphoglycerate mutase at 0.28 nm resolution

Structure:

Phosphoglycerate mutase 1. Chain: a, b. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932

Biol. unit:

Tetramer (from PQS)

Resolution:

2.80Å

R-factor:

not given

Authors:

J.W.Campbell,G.I.Hodgson,J.Warwicker,S.I.Winn,H.C.Watson

Key ref:

S.I.Winn et al. (1981). Structure and activity of phosphoglycerate mutase. Philos Trans R Soc Lond B Biol Sci, 293, 121-130. PubMed id: 6115412

Date:

06-Apr-82

Release date:

26-May-82

Supersedes:

1pgm

PROCHECK

	Headers

	References

Protein chains

P00950 (PMG1_YEAST) - Phosphoglycerate mutase 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: Struc:					247 a.a. 230 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 11 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

E.C.5.4.2.11 - phosphoglycerate mutase (2,3-diphosphoglycerate-dependent).

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

Reaction:

(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate

2-phospho-D-glycerate	=	3-phospho-D-glycerate

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

Added reference

	Philos Trans R Soc Lond B Biol Sci 293:121-130 (1981)
PubMed id: 6115412

Structure and activity of phosphoglycerate mutase.
S.I.Winn, H.C.Watson, R.N.Harkins, L.A.Fothergill.

ABSTRACT

The structure of yeast phosphoglycerate mutase determined by X-ray crystallographic and amino acid sequence studies has been interpreted in terms of the chemical, kinetic and mechanistic observations made on this enzyme. There are two histidine residues at the active site, with imidazole groups almost parallel to each other and approximately 0.4 nm apart, positioned close to the 2 and 3 positions of the substrate. The simplest interpretation of the available information suggests that a ping-pong type mechanism operates in which at least one of these histidine residues participates in the phosphoryl transfer reaction. The flexible C-terminal region also plays an important role in the enzymic reaction.

Literature references that cite this PDB file's key reference

PubMed id

Reference

17052986

Y.Wang, L.Liu, Z.Wei, Z.Cheng, Y.Lin, and W.Gong (2006).
Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase.

J Biol Chem, 281, 39642-39648.

PDB codes:

2a9j 2f90 2h4x 2h4z 2h52 2hhj

15258155

Y.Wang, Z.Wei, Q.Bian, Z.Cheng, M.Wan, L.Liu, and W.Gong (2004).
Crystal structure of human bisphosphoglycerate mutase.

J Biol Chem, 279, 39132-39138.

PDB code:

1t8p

9890980

M.H.Yuen, H.Mizuguchi, Y.H.Lee, P.F.Cook, K.Uyeda, and C.A.Hasemann (1999).
Crystal structure of the H256A mutant of rat testis fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase. Fructose 6-phosphate in the active site leads to mechanisms for both mutant and wild type bisphosphatase activities.

J Biol Chem, 274, 2176-2184.

PDB code:

2bif

9164457

D.Kostrewa, F.Grüninger-Leitch, A.D'Arcy, C.Broger, D.Mitchell, and A.P.van Loon (1997).
Crystal structure of phytase from Aspergillus ficuum at 2.5 A resolution.

Nat Struct Biol, 4, 185-190.

PDB code:

1ihp

7549867

I.J.Kurland, and S.J.Pilkis (1995).
Covalent control of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: insights into autoregulation of a bifunctional enzyme.

Protein Sci, 4, 1023-1037.

7768882

Y.Lan, T.Lu, P.S.Lovett, and D.J.Creighton (1995).
Evidence for a (triosephosphate isomerase-like) "catalytic loop" near the active site of glyoxalase I.

J Biol Chem, 270, 12957-12960.

8170953

M.C.Garel, N.Arous, M.C.Calvin, C.T.Craescu, J.Rosa, and R.Rosa (1994).
A recombinant bisphosphoglycerate mutase variant with acid phosphatase homology degrades 2,3-diphosphoglycerate.

Proc Natl Acad Sci U S A, 91, 3593-3597.

8334986

G.Schneider, Y.Lindqvist, and P.Vihko (1993).
Three-dimensional structure of rat acid phosphatase.

EMBO J, 12, 2609-2615.

8320209

L.P.Yomano, R.K.Scopes, and L.O.Ingram (1993).
Cloning, sequencing, and expression of the Zymomonas mobilis phosphoglycerate mutase gene (pgm) in Escherichia coli.

J Bacteriol, 175, 3926-3933.

8447317

S.Tsujino, S.Shanske, S.Sakoda, G.Fenichel, and S.DiMauro (1993).
The molecular genetic basis of muscle phosphoglycerate mutase (PGAM) deficiency.

Am J Hum Genet, 52, 472-477.

1530847

P.J.White, J.Nairn, N.C.Price, H.G.Nimmo, J.R.Coggins, and I.S.Hunter (1992).
Phosphoglycerate mutase from Streptomyces coelicolor A3(2): purification and characterization of the enzyme and cloning and sequence analysis of the gene.

J Bacteriol, 174, 434-440.

2557623

J.F.Bazan, R.J.Fletterick, and S.J.Pilkis (1989).
Evolution of a bifunctional enzyme: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.

Proc Natl Acad Sci U S A, 86, 9642-9646.

6313356

N.W.Haggarty, B.Dunbar, and L.A.Fothergill (1983).
The complete amino acid sequence of human erythrocyte diphosphoglycerate mutase.

EMBO J, 2, 1213-1220.

6765200

H.C.Watson, N.P.Walker, P.J.Shaw, T.N.Bryant, P.L.Wendell, L.A.Fothergill, R.E.Perkins, S.C.Conroy, M.J.Dobson, and M.F.Tuite (1982).
Sequence and structure of yeast phosphoglycerate kinase.

EMBO J, 1, 1635-1640.

PDB code:

3pgk

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 codes are shown on the right.