5XJO

Plant receptor ERL1-TMM in complex with peptide EPF1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.63 Å
  • R-Value Free: 0.310 
  • R-Value Work: 0.252 
  • R-Value Observed: 0.255 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

A receptor-like protein acts as a specificity switch for the regulation of stomatal development.

Lin, G.Zhang, L.Han, Z.Yang, X.Liu, W.Li, E.Chang, J.Qi, Y.Shpak, E.D.Chai, J.

(2017) Genes Dev 31: 927-938

  • DOI: https://doi.org/10.1101/gad.297580.117
  • Primary Citation of Related Structures:  
    5XJO, 5XJX, 5XKJ, 5XKN

  • PubMed Abstract: 

    Stomata are microscopic openings that allow for the exchange of gases between plants and the environment. In Arabidopsis , stomatal patterning is specified by the ERECTA family (ERf) receptor kinases (RKs), the receptor-like protein (RLP) TOO MANY MOUTHS (TMM), and EPIDERMAL PATTERNING FACTOR (EPF) peptides. Here we show that TMM and ER or ER-LIKE1 (ERL1) form constitutive complexes, which recognize EPF1 and EPF2, but the single ERfs do not. TMM interaction with ERL1 creates a binding pocket for recognition of EPF1 and EPF2, indicating that the constitutive TMM-ERf complexes function as the receptors of EPF1 and EPF2. EPFL9 competes with EPF1 and EPF2 for binding to the ERf-TMM complex. EPFL4 and EPFL6, however, are recognized by the single ERfs without the requirement of TMM. In contrast to EPF1,2, the interaction of EPFL4,6 with an ERf is greatly reduced in the presence of TMM. Taken together, our data demonstrate that TMM dictates the specificity of ERfs for the perception of different EPFs, thus functioning as a specificity switch for the regulation of the activities of ERfs.


  • Organizational Affiliation

    Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
LRR receptor-like serine/threonine-protein kinase ERL1A,
F [auth B]
539Arabidopsis thalianaMutation(s): 0 
Gene Names: ERL1At5g62230MMI9.14
EC: 2.7.11.1
UniProt
Find proteins for C0LGW6 (Arabidopsis thaliana)
Explore C0LGW6 
Go to UniProtKB:  C0LGW6
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UniProt GroupC0LGW6
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Protein EPIDERMAL PATTERNING FACTOR 1B [auth F],
C [auth E]
52Arabidopsis thalianaMutation(s): 0 
Gene Names: EPF1At2g20875F5H14
UniProt
Find proteins for Q8S8I4 (Arabidopsis thaliana)
Explore Q8S8I4 
Go to UniProtKB:  Q8S8I4
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UniProt GroupQ8S8I4
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Protein TOO MANY MOUTHSD [auth C],
E [auth D]
374Arabidopsis thalianaMutation(s): 0 
Gene Names: TMMRLP17At1g80080F18B13.16
UniProt
Find proteins for Q9SSD1 (Arabidopsis thaliana)
Explore Q9SSD1 
Go to UniProtKB:  Q9SSD1
Entity Groups  
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UniProt GroupQ9SSD1
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.63 Å
  • R-Value Free: 0.310 
  • R-Value Work: 0.252 
  • R-Value Observed: 0.255 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 66.11α = 97.61
b = 66.147β = 102.47
c = 143.485γ = 93.68
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data scaling
PHASERphasing

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Natural Science Foundation of ChinaChina31420103906

Revision History  (Full details and data files)

  • Version 1.0: 2019-01-23
    Type: Initial release