2HPR

HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR MUTANT WITH MET 51 REPLACED BY VAL AND SER 83 REPLACED BY CYS (M51V, S83C)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Observed: 0.145 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Refined structures of the active Ser83-->Cys and impaired Ser46-->Asp histidine-containing phosphocarrier proteins.

Liao, D.I.Herzberg, O.

(1994) Structure 2: 1203-1216

  • DOI: https://doi.org/10.1016/s0969-2126(94)00122-7
  • Primary Citation of Related Structures:  
    1SPH, 2HPR

  • PubMed Abstract: 

    The histidine-containing phosphocarrier protein (HPr) functions in the bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS). His15 on HPr accepts a phosphoryl group from Enzyme I and transfers it to the Enzyme IIA domain of a sugar-specific PTS permease. In addition, HPrs from Gram-positive bacteria undergo phosphorylation on a serine residue, Ser46, which inhibits phosphorylation at His15 and sugar transport. The questions to be addressed at the molecular level are: what is the mechanism of each of the phosphoryl transfers and what conformational transitions are associated with each event? Thus, the crystal structures of the mutants Ser83-->Cys HPr (fully active protein) and Ser46-->Asp HPr (impaired protein which mimics Ser46 approximately P HPr) from Bacillus subtilis have been determined at 2 A resolution. They have been crystallized from high-salt and low-salt solutions respectively, and in two different space groups. Analysis of the two crystal forms reveals some significant differences but these do not alter the overall fold of the protein. In each structure, the side chain of His15 caps the following helix. Two alternative side-chain conformations of Arg17 are observed; it either forms an ion pair with a sulfate ion, presumably resembling the phosphorylated state of the protein (high-salt crystal) or with Glu84 (low-salt crystal). The main-chain conformation in the region of residue 46 is the same in the two crystal forms, with both Ser46 and Asp46 capping the following helix. The analysis suggests that phosphorylation of either His15 or Ser46 is not associated with main-chain conformational transitions. Rather, the protein is poised to accept the respective phosphoryl group with minor adjustments to side chains. The inhibitory effect of phosphorylation on Ser46 is attributed to the altered surface electrostatics, which impairs protein-protein interaction.


  • Organizational Affiliation

    Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville 20850.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR87Bacillus subtilisMutation(s): 0 
UniProt
Find proteins for P08877 (Bacillus subtilis (strain 168))
Explore P08877 
Go to UniProtKB:  P08877
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP08877
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SO4
Query on SO4

Download Ideal Coordinates CCD File 
B [auth A]SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
CSO
Query on CSO
A
L-PEPTIDE LINKINGC3 H7 N O3 SCYS
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Observed: 0.145 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 47.26α = 90
b = 47.26β = 90
c = 61.85γ = 120
Software Package:
Software NamePurpose
PROLSQrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

  • Released Date: 1993-01-15 
  • Deposition Author(s): Herzberg, O.

Revision History  (Full details and data files)

  • Version 1.0: 1993-01-15
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2024-06-05
    Changes: Data collection, Database references, Derived calculations, Other