PDBsum entry 2h4x

Isomerase

PDB id: 2h4x

Contents

Protein chain

255 a.a. *

Ligands

3PG ×2

Waters ×698

* Residue conservation analysis

PDB id:

2h4x

Name:

Isomerase

Title:

Human bisphosphoglycerate mutase complex with 3-phosphoglycerate with crystal growth 90 days

Structure:

Bisphosphoglycerate mutase. Chain: a, b. Synonym: 2,3-bisphosphoglycerate mutase, erythrocyte, 2,3- bisphosphoglycerate synthase, bpgm, bpg-dependent pgam. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Dimer (from PQS)

Resolution:

1.85Å R-factor: 0.180 R-free: 0.215

Authors:

Y.Wang,W.Gong

Key ref:

Y.Wang et al. (2006). Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase. J Biol Chem, 281, 39642-39648. PubMed id: 17052986 DOI: 10.1074/jbc.M606421200

Date:

25-May-06 Release date: 24-Oct-06

Protein chains

P07738  (PMGE_HUMAN) -  Bisphosphoglycerate mutase from Homo sapiens

Seq: 259 a.a.

Struc: 255 a.a.

Enzyme reactions

• Enzyme class 2: E.C.5.4.2.11 - phosphoglycerate mutase (2,3-diphosphoglycerate-dependent).
• Reaction: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
• Enzyme class 3: E.C.5.4.2.4 - bisphosphoglycerate mutase.
• Reaction: (2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-bisphosphoglycerate + H⁺

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.M606421200

J Biol Chem 281:39642-39648 (2006)

PubMed id: 17052986

Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase.

Y.Wang, L.Liu, Z.Wei, Z.Cheng, Y.Lin, W.Gong.

ABSTRACT

Bisphosphoglycerate mutase is an erythrocyte-specific enzyme catalyzing a series of intermolecular phosphoryl group transfer reactions. Its main function is to synthesize 2,3-bisphosphoglycerate, the allosteric effector of hemoglobin. In this paper, we directly observed real-time motion of the enzyme active site and the substrate during phosphoryl transfer. A series of high resolution crystal structures of human bisphosphoglycerate mutase co-crystallized with 2,3-bisphosphoglycerate, representing different time points in the phosphoryl transfer reaction, were solved. These structures not only clarify the argument concerning the substrate binding mode for this enzyme family but also depict the entire process of the key histidine phosphorylation as a "slow movie". It was observed that the enzyme conformation continuously changed during the different states of the reaction. These results provide direct evidence for an "in line" phosphoryl transfer mechanism, and the roles of some key residues in the phosphoryl transfer process are identified.

Selected figure(s)

Figure 1.
FIGURE 1. A F[o] - F[c] electron density map (contoured at 3.5 , purple cage) at the active site when the side chain of His-11 and the ligand are omitted. A (structure 1), co-crystallized with 2,3-BPG at 4 °C. B (structure 2), co-crystallized with 2,3-BPG at 16 °C for less than 16 days. C (structure 3), only 3-PGA binding. D (structure 4), co-crystallized with 2,3-BPG at 16 °C for 17 days. Extra F[o] - F[c] electron density (contoured at 3 , blue cage) exists when two water molecules and 3-PGA are modeled in. E (structure 5), co-crystallized with and 3-PGA.

Figure 4.
FIGURE 4. Schematic of the interactions between the ligand and human BPGM with all interactions between the ligand and residues depicted as dashed lines and labeled with the bond lengths (Å). A, interactions between 2,3-BPG and BPGM in the reacting state. B, interaction between 3-PGA and the phosphorylated enzyme.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2006, 281, 39642-39648) copyright 2006.

Figures were selected by an automated process.