Thirty-four of the 85 residues of the histidine-containing protein HPr of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system have been changed by site-directed mutagenesis. Many of the mutations have wild-type activity suggesting an unaltered tertiary structure but have altered binding to three monoclonal antibodies: Jel42, Jel44, and Jel323. This altered binding defines the residues that are involved in the epitopes of HPr. At present, two different three-dimensional structures have been determined for HPr, one from two-dimensional nuclear magnetic resonance spectra and the other from x-ray diffraction of HPr crystals. The epitope mapping for Jel42 does not distinguish between the tertiary structures. However, only the HPr structure derived from two-dimensional nuclear magnetic resonance spectra is consistent with a contiguous surface binding site that can be defined as the epitope for Jel44. Thus the x-ray structure may represent a partially unfolded HPr.
ID: xawcnBDF
Submitter: Shu-Ching Ou
Submission Date: Feb. 27, 2019, 12:36 p.m.
Version: 1
Sequences for Jel44 and Jel323 are not found, thus the sequences/mutants associated with the binding data do not include sequences of these two monoclonal antibodies.
Colors: | D | E | R | H | K | S | T | N | Q | A | V | I | L | M | F | Y | W | C | G | P |
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Percent Identity | Matching Chains | Protein | Accession | Entry Name |
---|---|---|---|---|
100.0 | Phosphocarrier protein HPr | P0AA06 | PTHP_ECO57 | |
100.0 | Phosphocarrier protein HPr | P0AA05 | PTHP_ECOL6 | |
100.0 | Phosphocarrier protein HPr | P0AA04 | PTHP_ECOLI | |
100.0 | Phosphocarrier protein HPr | P0AA08 | PTHP_SALTI | |
100.0 | Phosphocarrier protein HPr | P0AA07 | PTHP_SALTY | |
100.0 | Phosphocarrier protein HPr | P0AA09 | PTHP_SHIFL | |
98.8 | Phosphocarrier protein HPr | P16481 | PTHP_KLEPN |