PDBsum entry 2fkf

Isomerase

PDB id: 2fkf

Contents

Protein chain

455 a.a. *

Ligands

G16

Metals

_ZN

Waters ×296

* Residue conservation analysis

PDB id:

2fkf

Name:

Isomerase

Title:

Phosphomannomutase/phosphoglucomutase from pseudomonas aeruginosa with alpha-d-glucose 1,6-bisphosphate bound

Structure:

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

Source:

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

Resolution:

2.00Å R-factor: 0.253 R-free: 0.240

Authors:

C.A.Regni,L.J.Beamer

Key ref:

C.Regni et al. (2006). The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme. J Biol Chem, 281, 15564-15571. PubMed id: 16595672 DOI: 10.1074/jbc.M600590200

Date:

04-Jan-06 Release date: 04-Apr-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 = G16) matches with 80.00% 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 = G16) matches with 80.00% 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: 10.1074/jbc.M600590200

J Biol Chem 281:15564-15571 (2006)

PubMed id: 16595672

The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme.

C.Regni, A.M.Schramm, L.J.Beamer.

ABSTRACT

The enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from Pseudomonas aeruginosa catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars. The reaction entails two phosphoryl transfers, with an intervening 180 degrees reorientation of the reaction intermediate (e.g. glucose 1,6-bisphosphate) during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is, thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Structural characterization of two PMM/PGM-intermediate complexes with glucose 1,6-bisphosphate provides new insights into the reaction catalyzed by the enzyme, including the reorientation of the intermediate. Kinetic analyses of site-directed mutants prompted by the structural studies reveal active site residues critical for maintaining association with glucose 1,6-bisphosphate during its unique dynamic reorientation in the active site of PMM/PGM.

Selected figure(s)

Figure 2.
FIGURE 2. The final 2 F[o] – F[c] maps (blue, contoured at 1. 0 ) for G16P in the dephospho-PMM/PGM·G16P complex (a) and phospho-PMM/PGM·G16P complex (b). Electron density for Arg-15 and Arg-20 is also shown for this complex.

Figure 3.
FIGURE 3. a, superposition of the protein backbones for apo-PMM/PGM (Apo) and its complexes with G16P. DP, dephospho-PMM/PGM; P, phospho-PMM/PGM. Domains 1–4 are shown in green, yellow, red, and blue, respectively. G16P as bound to phosphoenzyme is shown in magenta and to dephosphoenzyme is shown in cyan. b, a close-up view of G16P in the active site of the two PMM/PGM-intermediate complexes showing their different relative binding positions. The protein backbone is shown in solid (dephosphoenzyme) and semitransparent (phosphoenzyme). Shown are hydrogen bonds between G16P and dephospho-PMM/PGM (c) and phospho-PMM/PGM (d). Protein residues that contact the intermediate are shown as sticks; water molecules are shown as blue spheres.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2006, 281, 15564-15571) copyright 2006.

Figures were selected by the author.