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PDBsum entry 4q3g
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PDB id:
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Transferase
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Title:
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Structure of the osserk2 leucine rich repeat extracellular domain
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Structure:
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Osserk2. Chain: a, b. Engineered: yes
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Source:
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Oryza sativa. Organism_taxid: 4530.
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Resolution:
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2.79Å
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R-factor:
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0.241
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R-free:
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0.277
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Authors:
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R.P.Mcandrew,R.N.Pruitt,S.G.Kamita,J.H.Pereira,D.Majumder, B.D.Hammock,P.D.Adams,P.C.Ronald
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Key ref:
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R.McAndrew
et al.
(2014).
Structure of the OsSERK2 leucine-rich repeat extracellular domain.
Acta Crystallogr D Biol Crystallogr,
70,
3080-3086.
PubMed id:
DOI:
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Date:
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11-Apr-14
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Release date:
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12-Nov-14
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PROCHECK
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Headers
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References
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Q01JP8
(Q01JP8_ORYSA) -
H0523F07.15 protein from Oryza sativa
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Seq:
Struc:
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628 a.a.
219 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 66 residue positions (black
crosses)
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DOI no:
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Acta Crystallogr D Biol Crystallogr
70:3080-3086
(2014)
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PubMed id:
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Structure of the OsSERK2 leucine-rich repeat extracellular domain.
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R.McAndrew,
R.N.Pruitt,
S.G.Kamita,
J.H.Pereira,
D.Majumdar,
B.D.Hammock,
P.D.Adams,
P.C.Ronald.
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ABSTRACT
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Somatic embryogenesis receptor kinases (SERKs) are leucine-rich repeat
(LRR)-containing integral membrane receptors that are involved in the regulation
of development and immune responses in plants. It has recently been shown that
rice SERK2 (OsSERK2) is essential for XA21-mediated resistance to the pathogen
Xanthomonas oryzae pv. oryzae. OsSERK2 is also required for the BRI1-mediated,
FLS2-mediated and EFR-mediated responses to brassinosteroids, flagellin and
elongation factor Tu (EF-Tu), respectively. Here, crystal structures of the LRR
domains of OsSERK2 and a D128N OsSERK2 mutant, expressed as hagfish variable
lymphocyte receptor (VLR) fusions, are reported. These structures suggest that
the aspartate mutation does not generate any significant conformational change
in the protein, but instead leads to an altered interaction with partner
receptors.
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Links
