PDBsum entry: 1pcj

Isomerase

PDB id: 1pcj

Contents

Protein chain

458 a.a. *

Ligands

M1P

Metals

_ZN

Waters ×310

* Residue conservation analysis

PDB id:

1pcj

Name:

Isomerase

Title:

Enzyme-ligand complex of p. Aeruginosa pmm/pgm

Structure:

Phosphomannomutase. Chain: x. Synonym: pmm. Engineered: yes

Source:

Pseudomonas aeruginosa. Organism_taxid: 287. Gene: algc or pa5322. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.00Å R-factor: 0.165 R-free: 0.203

Authors:

C.Regni,P.A.Tipton,L.J.Beamer

Key ref:

C.Regni et al. (2004). Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa. Structure, 12, 55-63. PubMed id: 14725765 DOI: 10.1016/j.str.2003.11.015

Date:

16-May-03 Release date: 20-Jan-04

Protein chain

P26276  (ALGC_PSEAE) -  Phosphomannomutase/phosphoglucomutase

Seq: 463 a.a.

Struc: 458 a.a.

Enzyme reactions

• Enzyme class 1: E.C.5.4.2.2 - Phosphoglucomutase.
• Pathway: UDP-glucose, UDP-galactose and UDP-glucuronate Biosynthesis
• Reaction: Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate

Alpha-D-glucose 1-phosphate (Bound ligand (Het Group name = M1P) corresponds exactly) = alpha-D-glucose 6-phosphate

• Enzyme class 2: E.C.5.4.2.8 - Phosphomannomutase.

Pathway:

• Reaction: Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate

Alpha-D-mannose 1-phosphate (Bound ligand (Het Group name = M1P) corresponds exactly) = D-mannose 6-phosphate

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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

 Gene Ontology (GO) functional annotation 

• Biological process: metabolic process (4 terms)
• Biochemical function: catalytic activity (7 terms)

reference

DOI no: 10.1016/j.str.2003.11.015

Structure 12:55-63 (2004)

PubMed id: 14725765

Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa.

C.Regni, L.Naught, P.A.Tipton, L.J.Beamer.

ABSTRACT

Enzyme-substrate complexes of phosphomannomutase/phosphoglucomutase (PMM/PGM) reveal the structural basis of the enzyme's ability to use four different substrates in catalysis. High-resolution structures with glucose 1-phosphate, glucose 6-phosphate, mannose 1-phosphate, and mannose 6-phosphate show that the position of the phosphate group of each substrate is held constant by a conserved network of hydrogen bonds. This produces two distinct, and mutually exclusive, binding orientations for the sugar rings of the 1-phospho and 6-phospho sugars. Specific binding of both orientations is accomplished by key contacts with the O3 and O4 hydroxyls of the sugar, which must occupy equatorial positions. Dual recognition of glucose and mannose phosphosugars uses a combination of specific protein contacts and nonspecific solvent contacts. The ability of PMM/PGM to accommodate these four diverse substrates in a single active site is consistent with its highly reversible phosphoryl transfer reaction and allows it to function in multiple biosynthetic pathways in P. aeruginosa.

Selected figure(s)

Figure 1.
Figure 1. Mechanism and Overall Structure of PMM/PGM(A) Mechanism of PMM/PGM shown in the biosynthetic direction of the reaction with G6P as the substrate.(B) Tube rendering of PMM/PGM and the G1P complex. The apo-protein and G1P complex were superimposed, and the areas differing between the two protein backbones are shown as a tube of varying diameter, proportional to the differences between the two structures. Domains 1 to 4 are shown in green (residues 1-153), yellow (residues 154-256), red (residues 257-368), and blue (residues 369-463), respectively.

The above figure is reprinted by permission from Cell Press: Structure (2004, 12, 55-63) copyright 2004.

Figure was selected by the author.