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PDBsum entry 4ic6
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PDB id:
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Hydrolase
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Title:
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Crystal structure of deg8
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Structure:
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Protease do-like 8, chloroplastic. Chain: a, b, c. Fragment: unp residues 91-448. Engineered: yes. Mutation: yes
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Source:
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Arabidopsis thaliana. Mouse-ear cress,thale-cress. Organism_taxid: 3702. Gene: degp8, at5g39830, k13h13.1. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.00Å
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R-factor:
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0.200
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R-free:
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0.235
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Authors:
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W.Gong,W.Sun,H.Fan,F.Gao,L.Liu
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Key ref:
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W.Sun
et al.
(2013).
The structures of Arabidopsis Deg5 and Deg8 reveal new insights into HtrA proteases.
Acta Crystallogr D Biol Crystallogr,
69,
830-837.
PubMed id:
DOI:
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Date:
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10-Dec-12
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Release date:
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01-May-13
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PROCHECK
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Headers
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References
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Q9LU10
(DEGP8_ARATH) -
Protease Do-like 8, chloroplastic from Arabidopsis thaliana
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Seq:
Struc:
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448 a.a.
340 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 1 residue position (black
cross)
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DOI no:
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Acta Crystallogr D Biol Crystallogr
69:830-837
(2013)
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PubMed id:
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The structures of Arabidopsis Deg5 and Deg8 reveal new insights into HtrA proteases.
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W.Sun,
F.Gao,
H.Fan,
X.Shan,
R.Sun,
L.Liu,
W.Gong.
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ABSTRACT
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Plant Deg5 and Deg8 are two members of the HtrA proteases, a family of
oligomeric serine endopeptidases that are involved in a variety of protein
quality-control processes. These two HtrA proteases are located in the thylakoid
lumen and participate in high-light stress responses by collaborating with other
chloroplast proteins. Deg5 and Deg8 degrade photodamaged D1 protein of the
photosystem II reaction centre, allowing its in situ replacement. Here, the
crystal structures of Arabidopsis thaliana Deg5 (S266A) and Deg8 (S292A) are
reported at 2.6 and 2.0 Å resolution, respectively. The Deg5 trimer contains
two calcium ions in a central channel, suggesting a link between photodamage
control and calcium ions in chloroplasts. Previous structures of HtrA proteases
have indicated that their regulation usually requires C-terminal PDZ domain(s).
Deg5 is unique in that it contains no PDZ domain and the trimeric structure of
Deg5 (S266A) reveals a novel catalytic triad conformation. A similar triad
conformation is observed in the hexameric structure of the single
PDZ-domain-containing Deg8 (S292A). These findings suggest a novel activation
mechanism for plant HtrA proteases and provide structural clues to their
function in light-stress response.
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