7DSP

Anthranilate phosphoribosyltransferase variant Ser121Ala from Saccharomyces cerevisiae with Mg bound

  • Classification: TRANSFERASE
  • Organism(s): Saccharomyces cerevisiae S288C
  • Expression System: Escherichia coli
  • Mutation(s): Yes 

  • Deposited: 2020-12-31 Released: 2021-03-17 
  • Deposition Author(s): Wu, X.
  • Funding Organization(s): Ministry of Science and Technology (MoST, China), National Natural Science Foundation of China (NSFC)

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.208 
  • R-Value Work: 0.164 
  • R-Value Observed: 0.166 

Starting Model: experimental
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This is version 1.1 of the entry. See complete history


Literature

Crystal structures of anthranilate phosphoribosyltransferase from Saccharomyces cerevisiae.

Wu, X.Zhang, M.Kuang, Z.Yue, J.Xue, L.Zhu, M.Zhu, Z.Khan, M.H.Niu, L.

(2021) Acta Crystallogr F Struct Biol Commun 77: 61-69

  • DOI: https://doi.org/10.1107/S2053230X21001989
  • Primary Citation of Related Structures:  
    7DSJ, 7DSM, 7DSO, 7DSP, 7DSR

  • PubMed Abstract: 

    Anthranilate phosphoribosyltransferase (AnPRT) catalyzes the transfer of the phosphoribosyl group of 5'-phosphoribosyl-1'-pyrophosphate (PRPP) to anthranilate to form phosphoribosyl-anthranilate. Crystal structures of AnPRTs from bacteria and archaea have previously been determined; however, the structure of Saccharomyces cerevisiae AnPRT (ScAnPRT) still remains unsolved. Here, crystal structures of ScAnPRT in the apo form as well as in complex with its substrate PRPP and the substrate analogue 4-fluoroanthranilate (4FA) are presented. These structures demonstrate that ScAnPRT exhibits the conserved structural fold of type III phosphoribosyltransferase enzymes and shares the similar mode of substrate binding found across the AnPRT protein family. In addition, crystal structures of ScAnPRT mutants (ScAnPRT Ser121Ala and ScAnPRT Gly141Asn ) were also determined. These structures suggested that the conserved residue Ser121 is critical for binding PRPP, while Gly141 is dispensable for binding 4FA. In summary, these structures improved the preliminary understanding of the substrate-binding mode of ScAnPRT and laid foundations for future research.


  • Organizational Affiliation

    School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Anthranilate phosphoribosyltransferaseA [auth B],
B [auth A]
383Saccharomyces cerevisiae S288CMutation(s): 1 
Gene Names: TRP4YDR354WD9476.4
EC: 2.4.2.18
UniProt
Find proteins for P07285 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P07285 
Go to UniProtKB:  P07285
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP07285
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.208 
  • R-Value Work: 0.164 
  • R-Value Observed: 0.166 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 79.164α = 90
b = 87.002β = 90
c = 108.433γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
PDB_EXTRACTdata extraction
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing

Structure Validation

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Entry History & Funding Information

Deposition Data

  • Released Date: 2021-03-17 
  • Deposition Author(s): Wu, X.

Funding OrganizationLocationGrant Number
Ministry of Science and Technology (MoST, China)China2017YFA0504903
National Natural Science Foundation of China (NSFC)China31621002

Revision History  (Full details and data files)

  • Version 1.0: 2021-03-17
    Type: Initial release
  • Version 1.1: 2023-11-29
    Changes: Data collection, Database references, Refinement description