PDBsum entry 2xdf

Transferase

PDB id: 2xdf

Contents

Protein chains

573 a.a. *

85 a.a. *

* Residue conservation analysis

PDB id:

2xdf

Name:

Transferase

Title:

Solution structure of the enzyme i dimer complexed with hpr using residual dipolar couplings and small angle x-ray scattering

Structure:

Phosphoenolpyruvate-protein phosphotransferase. Chain: a, b. Synonym: phosphotransferase system enzyme i. Engineered: yes. Phosphocarrier protein hpr. Chain: c, d. Synonym: histidine-containing phosphocarrier protein hpr. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 469008. Strain: bl21 star (de3). Expressed in: escherichia coli. Expression_system_taxid: 469008.

NMR struc:

2 models

Authors:

C.D.Schwieters,J.-Y.Suh,A.Grishaev,R.Guirlando,Y.Takayama,G.M.Clore

Key ref:

C.D.Schwieters et al. (2010). Solution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering. J Am Chem Soc, 132, 13026-13045. PubMed id: 20731394

Date:

30-Apr-10 Release date: 22-Sep-10

Protein chains

P08839  (PT1_ECOLI) -  Phosphoenolpyruvate-protein phosphotransferase from Escherichia coli (strain K12)

Seq: 575 a.a.

Struc: 573 a.a.

Protein chains

P0AA04  (PTHP_ECOLI) -  Phosphocarrier protein HPr from Escherichia coli (strain K12)

Seq: 85 a.a.

Struc: 85 a.a.

Enzyme reactions

• Enzyme class 2: Chains A, B: E.C.2.7.3.9 - phosphoenolpyruvate--protein phosphotransferase.
• Reaction: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl- [protein] + pyruvate
• Enzyme class 3: Chains C, D: E.C.2.7.11.- - ?????

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

Added reference

J Am Chem Soc 132:13026-13045 (2010)

PubMed id: 20731394

Solution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering.

C.D.Schwieters, J.Y.Suh, A.Grishaev, R.Ghirlando, Y.Takayama, G.M.Clore.

ABSTRACT

No abstract given.