Epitope mapping by mutagenesis distinguishes between the two tertiary structures of the histidine-containing protein HPr.
Abstract
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.
Submission Details
ID: xawcnBDF
Submitter: Shu-Ching Ou
Submission Date: Feb. 27, 2019, 12:36 p.m.
Version: 1
Publication Details
Sharma S;Georges F;Delbaere LT;Lee JS;Klevit RE;Waygood EB,Proc Natl Acad Sci U S A (1991) Epitope mapping by mutagenesis distinguishes between the two tertiary structures of the histidine-containing protein HPr. PMID:1711212Additional Information
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.
Study Summary
Structure view and single mutant data analysis
Study data
| Colors: | D | E | R | H | K | S | T | N | Q | A | V | I | L | M | F | Y | W | C | G | P |
|---|
Data Distribution
Studies with similar sequences (approximate matches)
Correlation with other assays (exact sequence matches)
Relevant PDB Entries
| Structure ID | Release Date | Resolution | Structure Title |
|---|---|---|---|
| 1CM2 | 1999-05-13T00:00:00+0000 | 1.8 | STRUCTURE OF HIS15ASP HPR AFTER HYDROLYSIS OF RINGED SPECIES. |
| 1CM3 | 1999-05-13T00:00:00+0000 | 1.6 | HIS15ASP HPR FROM E. COLI |
| 1GGR | 2000-09-18T00:00:00+0000 | 0 | COMPLEX OF ENZYME IIAGLC AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE |
| 1HDN | 1994-02-10T00:00:00+0000 | 0 | THE HIGH-RESOLUTION STRUCTURE OF THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI DETERMINED BY RESTRAINED MOLECULAR DYNAMICS FROM NMR NUCLEAR OVERHAUSER EFFECT DATA |
| 1J6T | 2002-08-14T00:00:00+0000 | 0 | COMPLEX OF ENZYME IIAMTL AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE |
| 1OPD | 1996-08-01T00:00:00+0000 | 1.5 | HISTIDINE-CONTAINING PROTEIN (HPR), MUTANT WITH SER 46 REPLACED BY ASP (S46D) |
| 1PFH | 1995-08-18T00:00:00+0000 | 0 | THE PHOSPHORYLATED FORM OF THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR |
| 1POH | 1993-10-19T00:00:00+0000 | 2.0 | THE 2.0 ANGSTROMS RESOLUTION STRUCTURE OF ESCHERICHIA COLI HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR: A REDETERMINATION |
| 1VRC | 2005-02-21T00:00:00+0000 | 0 | Complex of enzyme IIAmannose and the histidine-containing phosphocarrier protein HPr from escherichia coli nmr, restrained regularized mean structure |
| 2JEL | 1998-02-24T00:00:00+0000 | 2.5 | JEL42 FAB/HPR COMPLEX |
Relevant UniProtKB Entries
| 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 |