PDBsum entry: 3ezb

Transferase

PDB id: 3ezb

Contents

Protein chains

259 a.a. *

85 a.a. *

* Residue conservation analysis

PDB id:

3ezb

Name:

Transferase

Title:

Complex of the amino terminal domain of enzyme i and the histidine-containing phosphocarrier protein hpr from escherichia coli

Structure:

Protein (phosphotransfer system, enzyme i). Chain: a. Fragment: amino-terminal domain residues 1 - 259. Engineered: yes. Protein (phosphocarrier protein hpr). Chain: b. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Strain: gi698. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

40 models

Authors:

G.M.Clore,D.S.Garrett,A.M.Gronenborn

Key ref:

D.S.Garrett et al. (1999). Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr. Nat Struct Biol, 6, 166-173. PubMed id: 10048929 DOI: 10.1038/5854

Date:

03-Nov-98 Release date: 16-Dec-99

Supersedes:

3ezd

Protein chain

P08839  (PT1_ECOLI) -  Phosphoenolpyruvate-protein phosphotransferase

Seq: 575 a.a.

Struc: 259 a.a.*

Protein chain

P0AA04  (PTHP_ECOLI) -  Phosphocarrier protein HPr

Seq: 85 a.a.

Struc: 85 a.a.

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: Chain A: E.C.2.7.3.9 - Phosphoenolpyruvate--protein phosphotransferase.
• Reaction: Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)- phospho-L-histidine

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

 Gene Ontology (GO) functional annotation 

• Cellular component: cytoplasm (1 term)
• Biological process: transport (4 terms)
• Biochemical function: protein binding (7 terms)

reference

DOI no: 10.1038/5854

Nat Struct Biol 6:166-173 (1999)

PubMed id: 10048929

Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr.

D.S.Garrett, Y.J.Seok, A.Peterkofsky, A.M.Gronenborn, G.M.Clore.

ABSTRACT

The solution structure of the first protein-protein complex of the bacterial phosphoenolpyruvate: sugar phosphotransferase system between the N-terminal domain of enzyme I (EIN) and the histidine-containing phosphocarrier protein HPr has been determined by NMR spectroscopy, including the use of residual dipolar couplings that provide long-range structural information. The complex between EIN and HPr is a classical example of surface complementarity, involving an essentially all helical interface, comprising helices 2, 2', 3 and 4 of the alpha-subdomain of EIN and helices 1 and 2 of HPr, that requires virtually no changes in conformation of the components relative to that in their respective free states. The specificity of the complex is dependent on the correct placement of both van der Waals and electrostatic contacts. The transition state can be formed with minimal changes in overall conformation, and is stabilized in favor of phosphorylated HPr, thereby accounting for the directionality of phosphoryl transfer.

Selected figure(s)

Figure 2.
Figure 2. Structure of the EIN−HPr complex. a, Superposition of the backbone (N, C , C atoms) of the 40 simulated annealing structures of the EIN−HPr complex. b, Ribbon diagrams illustrating two views of the EIN−HPr complex. HPr is shown in green, the domain of EIN in red, and the / domain and C−terminal helix of EIN in blue. Also shown in (b) in gold are the side chains of His 189 of EIN and His 15' of HPr. Residues 1−250 of EIN and 1−85 of HPr are displayed.

Figure 3.
Figure 3. EIN−HPr interactions. a, Stereo view of the EIN−HPr interface. The backbones of EIN and HPr, depicted as a ribbon diagram, are shown in blue and dark green, respectively; the side chains of EIN and HPr are shown in red and light green, respectively; and His 15' of HPr is shown in gold. Residues of EIN and HPr are labeled in red and green, respectively. b, Summary of electrostatic (top) and van der Waals (bottom) interactions between EIN and HPr. The red lines indicate interactions between helix 1 of HPr and helix 4 of EIN, the green lines between helices 1 and 2 of HPr and helices 2 and 2' of EIN, and the blue lines between helix 2 of HPr and helices 3 and 4 of EIN. The dashed red lines for the electrostatic interactions represent side chain−backbone hydrogen bonds.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (1999, 6, 166-173) copyright 1999.

Figures were selected by an automated process.