1SPH

REFINED STRUCTURES OF THE ACTIVE S83C AND IMPAIRED S46D HPRS: EVIDENCE THAT PHOSPHORYLATION DOES NOT REQUIRE A BACKBONE CONFORMATIONAL TRANSITION

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Work: 0.143 
  • R-Value Observed: 0.143 

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This is version 1.5 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?

    • Organizational Affiliation: 

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


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR
A, B
88Bacillus subtilisMutation(s): 0 
Gene Names: PTSH
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
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Work: 0.143 
  • R-Value Observed: 0.143 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 49.5α = 90
b = 25.7β = 108.9
c = 60.4γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
TNTrefinement
X-PLORrefinement
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1995-02-07
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-07-17
    Changes: Data collection, Other, Refinement description
  • Version 1.4: 2019-08-14
    Changes: Data collection, Refinement description
  • Version 1.5: 2024-02-14
    Changes: Data collection, Database references