+Open data
-Basic information
Entry | Database: SASBDB / ID: SASDAD8 |
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Sample | Antiapoptotic membrane protein, (DpV84gp022) Deerpox virus
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Function / homology | Poxvirus F1/C10 / Apoptosis regulator M11L like / symbiont-mediated suppression of host apoptosis / Bcl-2-like superfamily / regulation of apoptotic process / membrane / Antiapoptotic membrane protein Function and homology information |
Biological species | Deerpox virus W-1170-84 |
Citation | Journal: Acta Crystallogr D Biol Crystallogr / Year: 2015 Title: Structural basis of Deerpox virus-mediated inhibition of apoptosis. Authors: Denis R Burton / Sofia Caria / Bevan Marshall / Michele Barry / Marc Kvansakul / Abstract: Apoptosis is a key innate defence mechanism to eliminate virally infected cells. To counteract premature host-cell apoptosis, poxviruses have evolved numerous molecular strategies, including the use ...Apoptosis is a key innate defence mechanism to eliminate virally infected cells. To counteract premature host-cell apoptosis, poxviruses have evolved numerous molecular strategies, including the use of Bcl-2 proteins, to ensure their own survival. Here, it is reported that the Deerpox virus inhibitor of apoptosis, DPV022, only engages a highly restricted set of death-inducing Bcl-2 proteins, including Bim, Bax and Bak, with modest affinities. Structural analysis reveals that DPV022 adopts a Bcl-2 fold with a dimeric domain-swapped topology and binds pro-death Bcl-2 proteins via two conserved ligand-binding grooves found on opposite sides of the dimer. Structures of DPV022 bound to Bim, Bak and Bax BH3 domains reveal that a partial obstruction of the binding groove is likely to be responsible for the modest affinities of DPV022 for BH3 domains. These findings reveal that domain-swapped dimeric Bcl-2 folds are not unusual and may be found more widely in viruses. Furthermore, the modest affinities of DPV022 for pro-death Bcl-2 proteins suggest that two distinct classes of anti-apoptotic viral Bcl-2 proteins exist: those that are monomeric and tightly bind a range of death-inducing Bcl-2 proteins, and others such as DPV022 that are dimeric and only bind a very limited number of death-inducing Bcl-2 proteins with modest affinities. |
Contact author |
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-Structure visualization
-Downloads & links
-Data source
SASBDB page | SASDAD8 |
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-Related structure data
Related structure data | 4uf1C 4uf2C 4uf3C C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-External links
Related items in Molecule of the Month |
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-Models
-Sample
Sample | Name: Antiapoptotic membrane protein, (DpV84gp022) Deerpox virus Specimen concentration: 0.22-6.34 |
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Buffer | Name: HEPES / Concentration: 25.00 mM / pH: 7.5 / Composition: 150 mM NaCl |
Entity #186 | Type: protein / Description: Antiapoptotic membrane protein / Formula weight: 19.6 / Num. of mol.: 2 / Source: Deerpox virus W-1170-84 / References: UniProt: Q08FF8 Sequence: MGSSHHHHHH SQDMEAAIEF DEIVKKLLNI YINDICTTGE KRLLNNYEKS ILDRIYKSCE YIKKNYELDF NSMYNQININ DITTSDIKSK IIEALLIDSR PSVKLATLSF ISLIAEKWGE KNRAKIMEIL SNEIVEKISN NGKDFIDFID RDDDDIVDDY VLITNYLK |
-Experimental information
Beam | Instrument name: Australian Synchrotron SAXS/WAXS / City: Melbourne / 国: Australia / Shape: Point / Type of source: X-ray synchrotron / Dist. spec. to detc.: 1.6 mm | ||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 1M | ||||||||||||||||||||||||||||||
Scan | Title: Antiapoptotic membrane protein (DpV84gp022) / Measurement date: May 4, 2013 / Storage temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 30 / Unit: 1/nm /
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Distance distribution function P(R) | Sofotware P(R): GNOM 5.0 / Number of points: 175 /
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Result | Type of curve: single_conc /
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