3EZE: COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE

Citation:
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.
PDB ID: 3EZEDownload
MMDB ID: 12104
PDB Deposition Date: 1998/11/4
Updated in MMDB: 2012/10
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 3EZE
Label Count Molecule
Proteins (2 molecules)
1
Protein (Phosphotransferase System, Enzyme I)(Gene symbol: ptsI)
Molecule annotation
1
Protein (Phosphotransferase System, Hpr)(Gene symbol: ptsH)
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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