1PCH

STRUCTURAL EVIDENCE FOR THE EVOLUTIONARY DIVERGENCE OF MYCOPLASMA FROM GRAM-POSITIVE BACTERIA: THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Work: 0.170 
  • R-Value Observed: 0.170 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history. 


Literature

Structural evidence for the evolutionary divergence of mycoplasma from gram-positive bacteria: the histidine-containing phosphocarrier protein.

Pieper, U., Kapadia, G., Zhu, P.P., Peterkofsky, A., Herzberg, O.

(1995) Structure 3: 781-790

  • DOI: https://doi.org/10.1016/s0969-2126(01)00213-1
  • Primary Citation of Related Structures:  
    1PCH

  • PubMed Abstract: 

    The three-dimensional structures of histidine-containing phosphocarrier protein (HPr), a member of the phosphoenolpyruvate:sugar phosphotransferase system (PTS), have been determined from Gram-negative and Gram-positive bacteria. The structure of HPr reported here for Mycoplasma capricolum is the first protein structure to be determined for this class of organism. Comparative structural studies with the bacterial proteins highlight sequence-structure correlations relevant to proposals about the evolutionary origin of mycoplasmas.

    • Organizational Affiliation: 

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


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PHOSPHOCARRIER PROTEIN88Mycoplasma capricolumMutation(s): 0 
Gene Names: PTSH
UniProt
Find proteins for P45611 (Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154))
Explore P45611 
Go to UniProtKB:  P45611
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP45611
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
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Work: 0.170 
  • R-Value Observed: 0.170 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 32.2α = 90
b = 42.2β = 90
c = 52.4γ = 90
Software Package:
Software NamePurpose
SHELXL-93model building
X-PLORmodel building
SHELXL-93refinement
X-PLORrefinement
XENGENdata reduction
SHELXL-93phasing
X-PLORphasing

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1995-10-15
    Type: Initial release
  • Version 1.1: 2008-03-24
    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, Derived calculations