5WQ3

Crystal structure of type-II LOG from Corynebacterium glutamicum


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.178 
  • R-Value Observed: 0.180 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural basis for a novel type of cytokinin-activating protein

Seo, H.Kim, K.-J.

(2017) Sci Rep 7: 45985-45985

  • DOI: https://doi.org/10.1038/srep45985
  • Primary Citation of Related Structures:  
    5WQ3

  • PubMed Abstract: 

    The Lonely Guy (LOG) protein has been identified as a crucial enzyme involved in the production of cytokinins, which are important phytohormones, in plants and plant-interacting organisms. However, C. glutamicum has an isoform (Cg1261) of LOG that contains an extended N-terminal region compared to those of known LOGs, and this type of isoforms are also found in a variety of organisms. Nevertheless, these proteins are considered as lysine decarboxylases, without their functional characterization. To investigate the function of Cg1261, we determined its crystal structure at a resolution of 1.95 Å. Unlike known dimeric LOGs, Cg1261 was found to form a hexamer. The overall shape of the hexamer resembles a trillium flower, in which a twisted dimer constitutes each petal. The dimeric petal is well superposed with known LOG dimers, and its active site conformation is similar to those of LOG dimers, suggesting that the hexameric LOG-like protein also acts as a LOG. Biochemical and in vivo cytokinin production studies on Cg1261 confirms that Cg1261 functions as a cytokinin-activating protein. Phylogenetic tree analysis using 123 LOG-like proteins suggest that the LOG-like proteins can be categorized to the dimeric type-I LOG and the hexameric type-II LOG.


  • Organizational Affiliation

    School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University, Daegu 702-701, Republic of Korea.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Cytokinin riboside 5'-monophosphate phosphoribohydrolase
A, B, C
264Corynebacterium glutamicumMutation(s): 0 
Gene Names: Cg1261
EC: 3.2.2
UniProt
Find proteins for Q8NRE2 (Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025))
Explore Q8NRE2 
Go to UniProtKB:  Q8NRE2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8NRE2
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 6 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
1PE
Query on 1PE

Download Ideal Coordinates CCD File 
D [auth A]PENTAETHYLENE GLYCOL
C10 H22 O6
JLFNLZLINWHATN-UHFFFAOYSA-N
PGE
Query on PGE

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M [auth C]TRIETHYLENE GLYCOL
C6 H14 O4
ZIBGPFATKBEMQZ-UHFFFAOYSA-N
PO4
Query on PO4

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F [auth A]PHOSPHATE ION
O4 P
NBIIXXVUZAFLBC-UHFFFAOYSA-K
GOL
Query on GOL

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E [auth A]GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
EDO
Query on EDO

Download Ideal Coordinates CCD File 
G [auth B],
H [auth B],
I [auth B],
L [auth C]
1,2-ETHANEDIOL
C2 H6 O2
LYCAIKOWRPUZTN-UHFFFAOYSA-N
CL
Query on CL

Download Ideal Coordinates CCD File 
J [auth B],
K [auth B],
N [auth C],
O [auth C],
P [auth C]
CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.178 
  • R-Value Observed: 0.180 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 98.701α = 90
b = 173.623β = 90
c = 79.903γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
PDB_EXTRACTdata extraction
HKL-2000data processing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-04-12
    Type: Initial release
  • Version 1.1: 2017-04-19
    Changes: Database references
  • Version 1.2: 2020-09-16
    Changes: Derived calculations, Structure summary
  • Version 1.3: 2023-11-08
    Changes: Data collection, Database references, Refinement description