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PcrG protects the two long helical oligomerization domains of PcrV, by an interaction mediated by the intramolecular coiled-coil region of PcrG
EPrints@IICB
View Archive Info| Field | Value | |
| Title |
PcrG protects the two long helical oligomerization domains of PcrV, by an interaction mediated by the intramolecular coiled-coil region of PcrG
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| Creator |
Basu, Abhishek
Das, Urmisha Dey, Supratim Datta, Saumen |
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| Subject |
Structural Biology & Bioinformatics
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| Description |
PcrV is a hydrophilic translocator of type three secretion system (TTSS) and a structural component of the functional translocon. C-terminal helix of PcrV is essential for its oligomerization at the needle tip. Conformational changes within PcrV regulate the effector translocation. PcrG is a cytoplasmic regulator of TTSS and forms a high affinity complex with PcrV. C-terminal residues of PcrG control the effector secretion. |
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| Publisher |
Chemistry Central
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| Date |
2014
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://www.eprints.iicb.res.in/2012/1/BMC_STRUCTURAL_BIOLOGY__V_14__Article_Number_5;2014(16).pdf
Basu, Abhishek and Das, Urmisha and Dey, Supratim and Datta, Saumen (2014) PcrG protects the two long helical oligomerization domains of PcrV, by an interaction mediated by the intramolecular coiled-coil region of PcrG. BMC Structural Biology, 14 (5). ISSN 1472-6807 |
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| Relation |
http://www.eprints.iicb.res.in/2012/
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