PDBsum entry 2h4l

Isomerase

PDB id: 2h4l

Contents

Protein chain

455 a.a. *

Ligands

R1P

Metals

_ZN

Waters ×144

* Residue conservation analysis

PDB id:

2h4l

Name:

Isomerase

Title:

Complex of pmm/pgm with ribose 1-phosphate

Structure:

Phosphomannomutase/phosphoglucomutase. Chain: x. Synonym: pmm / pgm. Engineered: yes

Source:

Pseudomonas aeruginosa. Organism_taxid: 287. Gene: algc. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.40Å R-factor: 0.190 R-free: 0.259

Authors:

L.J.Beamer

Key ref:

C.Regni et al. (2006). Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor. Acta Crystallograph Sect F Struct Biol Cryst Commun, 62, 722-726. PubMed id: 16880541 DOI: 10.1107/S1744309106025887

Date:

24-May-06 Release date: 08-Aug-06

Protein chain

P26276  (ALGC_PSEAE) -  Phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

Seq: 463 a.a.

Struc: 455 a.a.

Enzyme reactions

• Enzyme class 1: E.C.5.4.2.2 - phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent).
• 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 = R1P) matches with 87.50% similarity) = 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 = R1P) matches with 87.50% similarity) = 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

reference

DOI no: 10.1107/S1744309106025887

Acta Crystallograph Sect F Struct Biol Cryst Commun 62:722-726 (2006)

PubMed id: 16880541

Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor.

C.Regni, G.S.Shackelford, L.J.Beamer.

ABSTRACT

Two complexes of the enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from Pseudomonas aeruginosa with a slow substrate and with an inhibitor have been characterized by X-ray crystallography. Both ligands induce an interdomain rearrangement in the enzyme that creates a highly buried active site. Comparisons with enzyme-substrate complexes show that the inhibitor xylose 1-phosphate utilizes many of the previously observed enzyme-ligand interactions. In contrast, analysis of the ribose 1-phosphate complex reveals a combination of new and conserved enzyme-ligand interactions for binding. The ability of PMM/PGM to accommodate these two pentose phosphosugars in its active site may be relevant for future efforts towards inhibitor design.

Selected figure(s)

Figure 2.
Figure 2 PMM/PGM in complex with X1P and R1P. The protein is colored by domain, with blue, light blue, pink and magenta for domains 1, 2, 3 and 4, respectively. (a) Ribbon diagram of PMM/PGM with X1P (yellow) and R1P (green) bound in the active site. (b) Superposition of the C^ atoms of the R1P complex with those of apo-PMM/PGM (PDB code 1k2y ) shown in gray, demonstrating the rotation of domain 4. Close-up view of the active site of PMM/PGM with bound (c) X1P and (d) R1P. For clarity, only interactions between side chains of the enzyme and ligands are highlighted; water molecules are shown as spheres. (e) For comparison, a superposition of the slow substrate R1P and a preferred substrate G1P (cyan) in the active site of PMM/PGM is shown.

The above figure is reprinted by permission from the IUCr: Acta Crystallograph Sect F Struct Biol Cryst Commun (2006, 62, 722-726) copyright 2006.

Figure was selected by the author.