1USY

ATP phosphoribosyl transferase (HisG:HisZ) complex from Thermotoga maritima


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.52 Å
  • R-Value Free: 0.287 
  • R-Value Work: 0.203 
  • R-Value Observed: 0.207 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Regulation of the Hetero-Octameric ATP Phosphoribosyl Transferase Complex from Thermotoga Maritima by a tRNA Synthetase-Like Subunit.

Vega, M.C.Zou, P.Fernandez, F.J.Murphy, G.E.Sterner, R.Popov, A.Wilmanns, M.

(2005) Mol Microbiol 55: 675

  • DOI: https://doi.org/10.1111/j.1365-2958.2004.04422.x
  • Primary Citation of Related Structures:  
    1USY

  • PubMed Abstract: 

    The molecular structure of the ATP phosphoribosyl transferase from the hyperthermophile Thermotoga maritima is composed of a 220 kDa hetero-octameric complex comprising four catalytic subunits (HisGS) and four regulatory subunits (HisZ). Steady-state kinetics indicate that only the complete octameric complex is active and non-competitively inhibited by the pathway product histidine. The rationale for these findings is provided by the crystal structure revealing a total of eight histidine binding sites that are located within each of the four HisGS-HisZ subunit interfaces formed by the ATP phosphoribosyl transferase complex. While the structure of the catalytic HisGS subunit is related to the catalytic domain of another family of (HisGL)2 ATP phosphoribosyl transferases that is functional in the absence of additional regulatory subunits, the structure of the regulatory HisZ subunit is distantly related to class II aminoacyl-tRNA synthetases. However, neither the mode of the oligomeric subunit arrangement nor the type of histidine binding pockets is found in these structural relatives. Common ancestry of the regulatory HisZ subunit and class II aminoacyl-tRNA synthetase may reflect the balanced need of regulated amounts of a cognate amino acid (histidine) in the translation apparatus, ultimately linking amino acid biosynthesis and protein biosynthesis in terms of function, structure and evolution.


  • Organizational Affiliation

    EMBL Hamburg Outstation, Notkestrasse 85, Building 25A, D-22603 Hamburg, Germany.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ATP PHOSPHORIBOSYLTRANSFERASE REGULATORY SUBUNIT
A, B, D
275Thermotoga maritima MSB8Mutation(s): 0 
UniProt
Find proteins for Q9X0D3 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
Explore Q9X0D3 
Go to UniProtKB:  Q9X0D3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9X0D3
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
ATP PHOSPHORIBOSYLTRANSFERASE REGULATORY SUBUNIT275Thermotoga maritima MSB8Mutation(s): 0 
UniProt
Find proteins for Q9X0D3 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
Explore Q9X0D3 
Go to UniProtKB:  Q9X0D3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9X0D3
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
ATP PHOSPHORIBOSYLTRANSFERASE
E, F, G
208Thermotoga maritima MSB8Mutation(s): 0 
EC: 2.4.2.17
UniProt
Find proteins for Q9X0D2 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
Explore Q9X0D2 
Go to UniProtKB:  Q9X0D2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9X0D2
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
ATP PHOSPHORIBOSYLTRANSFERASE208Thermotoga maritima MSB8Mutation(s): 0 
EC: 2.4.2.17
UniProt
Find proteins for Q9X0D2 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
Explore Q9X0D2 
Go to UniProtKB:  Q9X0D2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9X0D2
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
HIS
Query on HIS

Download Ideal Coordinates CCD File 
I [auth C]
J [auth D]
M [auth E]
N [auth E]
P [auth F]
I [auth C],
J [auth D],
M [auth E],
N [auth E],
P [auth F],
S [auth G],
U [auth H],
V [auth H]
HISTIDINE
C6 H10 N3 O2
HNDVDQJCIGZPNO-YFKPBYRVSA-O
PO4
Query on PO4

Download Ideal Coordinates CCD File 
K [auth E]
L [auth E]
O [auth F]
Q [auth G]
R [auth G]
K [auth E],
L [auth E],
O [auth F],
Q [auth G],
R [auth G],
T [auth H]
PHOSPHATE ION
O4 P
NBIIXXVUZAFLBC-UHFFFAOYSA-K
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.52 Å
  • R-Value Free: 0.287 
  • R-Value Work: 0.203 
  • R-Value Observed: 0.207 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 101.58α = 90
b = 134.403β = 90
c = 154.206γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
SOLVEphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-12-15
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2013-12-25
    Changes: Atomic model, Derived calculations, Other
  • Version 1.3: 2014-09-10
    Changes: Database references, Other