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==Human caspase 9 in complex with bacterial effector protein==
==Human caspase 9 in complex with bacterial effector protein==
<StructureSection load='3v3k' size='340' side='right' caption='[[3v3k]], [[Resolution|resolution]] 3.49&Aring;' scene=''>
<StructureSection load='3v3k' size='340' side='right'caption='[[3v3k]], [[Resolution|resolution]] 3.49&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3v3k]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o157:h7 Escherichia coli o157:h7] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V3K FirstGlance]. <br>
<table><tr><td colspan='2'>[[3v3k]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V3K FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CASP9, MCH6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), ECs1815, Z6020 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 Escherichia coli O157:H7])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.494&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Caspase-9 Caspase-9], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.62 3.4.22.62] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3v3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v3k OCA], [https://pdbe.org/3v3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v3k RCSB], [https://www.ebi.ac.uk/pdbsum/3v3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v3k ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3v3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v3k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v3k RCSB], [http://www.ebi.ac.uk/pdbsum/3v3k PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CASP9_HUMAN CASP9_HUMAN]] Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP).<ref>PMID:15657060</ref>  Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.<ref>PMID:15657060</ref> [[http://www.uniprot.org/uniprot/Q8XAL7_ECO57 Q8XAL7_ECO57]] Effector protein that alters host cell physiology and promotes bacterial survival in host tissues. Inhibits the catalytic activity of human CASP4, CASP8 and CASP9, and thereby inhibits apoptosis of infected host cells.<ref>PMID:18279332</ref> <ref>PMID:23516580</ref> 
[https://www.uniprot.org/uniprot/CASP9_HUMAN CASP9_HUMAN] Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP).<ref>PMID:15657060</ref>  Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.<ref>PMID:15657060</ref>  


==See Also==
==See Also==
*[[Caspase|Caspase]]
*[[Caspase 3D structures|Caspase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Caspase-9]]
[[Category: Escherichia coli O157:H7]]
[[Category: Escherichia coli o157:h7]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Maskos, K]]
[[Category: Large Structures]]
[[Category: Moertl, M]]
[[Category: Maskos K]]
[[Category: Steuber, H]]
[[Category: Moertl M]]
[[Category: Caspase 9]]
[[Category: Steuber H]]
[[Category: Hydrolase]]

Latest revision as of 13:30, 1 March 2024

Human caspase 9 in complex with bacterial effector proteinHuman caspase 9 in complex with bacterial effector protein

Structural highlights

3v3k is a 16 chain structure with sequence from Escherichia coli O157:H7 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.494Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CASP9_HUMAN Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP).[1] Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.[2]

See Also

References

  1. ↑ Raina D, Pandey P, Ahmad R, Bharti A, Ren J, Kharbanda S, Weichselbaum R, Kufe D. c-Abl tyrosine kinase regulates caspase-9 autocleavage in the apoptotic response to DNA damage. J Biol Chem. 2005 Mar 25;280(12):11147-51. Epub 2005 Jan 18. PMID:15657060 doi:10.1074/jbc.M413787200
  2. ↑ Raina D, Pandey P, Ahmad R, Bharti A, Ren J, Kharbanda S, Weichselbaum R, Kufe D. c-Abl tyrosine kinase regulates caspase-9 autocleavage in the apoptotic response to DNA damage. J Biol Chem. 2005 Mar 25;280(12):11147-51. Epub 2005 Jan 18. PMID:15657060 doi:10.1074/jbc.M413787200

3v3k, resolution 3.49Å

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