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| | ==CARDS TOXIN, FULL-LENGTH== | | ==CARDS TOXIN, FULL-LENGTH== |
| - | <StructureSection load='4tlw' size='340' side='right' caption='[[4tlw]], [[Resolution|resolution]] 2.55Å' scene=''> | + | <StructureSection load='4tlw' size='340' side='right'caption='[[4tlw]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4tlw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TLW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TLW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4tlw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycoplasma_pneumoniae_M129 Mycoplasma pneumoniae M129]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TLW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TLW FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tlv|4tlv]]</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]] 2.55Å</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=4tlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tlw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tlw RCSB], [http://www.ebi.ac.uk/pdbsum/4tlw PDBsum]</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=4tlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tlw OCA], [https://pdbe.org/4tlw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tlw RCSB], [https://www.ebi.ac.uk/pdbsum/4tlw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tlw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CARDS_MYCPN CARDS_MYCPN]] Acts as an ADP-ribosylating toxin, which may transfer the ADP-ribosyl group from NAD(+) to specific amino acids in target proteins. Elicits cytopathic effects in mammalian cells, such as disorganization and disruption of respiratory epithelial integrity in tracheal epithelium and vacuolization in the cytoplasm of CHO and HeLa cells.<ref>PMID:16617115</ref> | + | [https://www.uniprot.org/uniprot/CARDS_MYCPN CARDS_MYCPN] Acts as an ADP-ribosylating toxin, which may transfer the ADP-ribosyl group from NAD(+) to specific amino acids in target proteins. Elicits cytopathic effects in mammalian cells, such as disorganization and disruption of respiratory epithelial integrity in tracheal epithelium and vacuolization in the cytoplasm of CHO and HeLa cells.<ref>PMID:16617115</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4tlw" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Becker, A]] | + | [[Category: Large Structures]] |
| - | [[Category: GALALELDEEN, A]] | + | [[Category: Mycoplasma pneumoniae M129]] |
| - | [[Category: Hart, P J]] | + | [[Category: Becker A]] |
| - | [[Category: Taylor, A B]] | + | [[Category: GALALELDEEN A]] |
| - | [[Category: Adp-ribosyl transferase]] | + | [[Category: Hart PJ]] |
| - | [[Category: Atypical pneumonia]] | + | [[Category: Taylor AB]] |
| - | [[Category: Community acquired respiratory distress syndrome]]
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| - | [[Category: Mycoplasma pneumoniae]]
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| - | [[Category: Toxin]]
| + | |
| - | [[Category: Transferase]]
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| - | [[Category: Virulence]]
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| Structural highlights
Function
CARDS_MYCPN Acts as an ADP-ribosylating toxin, which may transfer the ADP-ribosyl group from NAD(+) to specific amino acids in target proteins. Elicits cytopathic effects in mammalian cells, such as disorganization and disruption of respiratory epithelial integrity in tracheal epithelium and vacuolization in the cytoplasm of CHO and HeLa cells.[1]
Publication Abstract from PubMed
Mycoplasma pneumoniae (Mp) infections cause tracheobronchitis and "walking" pneumonia, and are linked to asthma and other reactive airway diseases. As part of the infectious process, the bacterium expresses a 591-aa virulence factor with both mono-ADP ribosyltransferase (mART) and vacuolating activities known as Community-Acquired Respiratory Distress Syndrome Toxin (CARDS TX). CARDS TX binds to human surfactant protein A and annexin A2 on airway epithelial cells and is internalized, leading to a range of pathogenetic events. Here we present the structure of CARDS TX, a triangular molecule in which N-terminal mART and C-terminal tandem beta-trefoil domains associate to form an overall architecture distinct from other well-recognized ADP-ribosylating bacterial toxins. We demonstrate that CARDS TX binds phosphatidylcholine and sphingomyelin specifically over other membrane lipids, and that cell surface binding and internalization activities are housed within the C-terminal beta-trefoil domain. The results enhance our understanding of Mp pathogenicity and suggest a novel avenue for the development of therapies to treat Mp-associated asthma and other acute and chronic airway diseases.
Structure of CARDS toxin, a unique ADP-ribosylating and vacuolating cytotoxin from Mycoplasma pneumoniae.,Becker A, Kannan TR, Taylor AB, Pakhomova ON, Zhang Y, Somarajan SR, Galaleldeen A, Holloway SP, Baseman JB, Hart PJ Proc Natl Acad Sci U S A. 2015 Apr 6. pii: 201420308. PMID:25848012[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kannan TR, Baseman JB. ADP-ribosylating and vacuolating cytotoxin of Mycoplasma pneumoniae represents unique virulence determinant among bacterial pathogens. Proc Natl Acad Sci U S A. 2006 Apr 25;103(17):6724-9. Epub 2006 Apr 14. PMID:16617115 doi:http://dx.doi.org/0510644103
- ↑ Becker A, Kannan TR, Taylor AB, Pakhomova ON, Zhang Y, Somarajan SR, Galaleldeen A, Holloway SP, Baseman JB, Hart PJ. Structure of CARDS toxin, a unique ADP-ribosylating and vacuolating cytotoxin from Mycoplasma pneumoniae. Proc Natl Acad Sci U S A. 2015 Apr 6. pii: 201420308. PMID:25848012 doi:http://dx.doi.org/10.1073/pnas.1420308112
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