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PDBsum entry 3sip
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Hydrolase/ligase/hydrolase
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PDB id
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3sip
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Contents |
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149 a.a.
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100 a.a.
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108 a.a.
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103 a.a.
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PDB id:
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| Name: |
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Hydrolase/ligase/hydrolase
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Title:
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Crystal structure of drice and diap1-bir1 complex
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Structure:
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Caspase. Chain: a, c. Fragment: unp residues 78-230. Synonym: drice large subunit, drice, caspase subunit p21, caspase subunit p12. Engineered: yes. Apoptosis 1 inhibitor. Chain: e, f. Fragment: unp residues 31-145.
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Source:
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Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
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Resolution:
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3.50Å
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R-factor:
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0.212
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R-free:
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0.256
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Authors:
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X.Li,J.Wang,Y.Shi
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Key ref:
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X.Li
et al.
(2011).
Structural mechanisms of DIAP1 auto-inhibition and DIAP1-mediated inhibition of drICE.
Nat Commun,
2,
408.
PubMed id:
DOI:
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Date:
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20-Jun-11
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Release date:
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10-Aug-11
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PROCHECK
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Headers
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References
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O01382
(DRICE_DROME) -
Caspase from Drosophila melanogaster
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Seq:
Struc:
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339 a.a.
149 a.a.*
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Q24306
(DIAP1_DROME) -
Death-associated inhibitor of apoptosis 1 from Drosophila melanogaster
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Seq:
Struc:
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438 a.a.
100 a.a.*
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Enzyme class:
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Chains E, F:
E.C.2.3.2.27
- RING-type E3 ubiquitin transferase.
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Reaction:
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine
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DOI no:
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Nat Commun
2:408
(2011)
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PubMed id:
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Structural mechanisms of DIAP1 auto-inhibition and DIAP1-mediated inhibition of drICE.
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X.Li,
J.Wang,
Y.Shi.
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ABSTRACT
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The Drosophila inhibitor of apoptosis protein DIAP1 exists in an auto-inhibited
conformation, unable to suppress the effector caspase drICE. Auto-inhibition is
disabled by caspase-mediated cleavage of DIAP1 after Asp20. The cleaved DIAP1
binds to mature drICE, inhibits its protease activity, and, presumably, also
targets drICE for ubiquitylation. DIAP1-mediated suppression of drICE is
effectively antagonized by the pro-apoptotic proteins Reaper, Hid, and Grim
(RHG). Despite rigorous effort, the molecular mechanisms behind these
observations are enigmatic. Here we report a 2.4 Å crystal structure of
uncleaved DIAP1-BIR1, which reveals how the amino-terminal sequences recognize a
conserved surface groove in BIR1 to achieve auto-inhibition, and a 3.5 Å
crystal structure of active drICE bound to cleaved DIAP1-BIR1, which provides a
structural explanation to DIAP1-mediated inhibition of drICE. These structures
and associated biochemical analyses, together with published reports, define the
molecular determinants that govern the interplay among DIAP1, drICE and the RHG
proteins.
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Links
