5a9y: Difference between revisions
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<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=5a9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a9y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a9y RCSB], [http://www.ebi.ac.uk/pdbsum/5a9y PDBsum]</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=5a9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a9y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a9y RCSB], [http://www.ebi.ac.uk/pdbsum/5a9y PDBsum]</span></td></tr> | ||
</table> | </table> | ||
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== Publication Abstract from PubMed == | |||
BPI-inducible protein A (BipA) is a member of the family of ribosome-dependent translational GTPase (trGTPase) factors along with elongation factors G and 4 (EF-G and EF4). Despite being highly conserved in bacteria and playing a critical role in coordinating cellular responses to environmental changes, its structures (isolated and ribosome bound) remain elusive. Here, we present the crystal structures of apo form and GTP analog, GDP, and guanosine-3',5'-bisdiphosphate (ppGpp)-bound BipA. In addition to having a distinctive domain arrangement, the C-terminal domain of BipA has a unique fold. Furthermore, we report the cryo-electron microscopy structure of BipA bound to the ribosome in its active GTP form and elucidate the unique structural attributes of BipA interactions with the ribosome and A-site tRNA in the light of its possible function in regulating translation. | |||
Structure of BipA in GTP form bound to the ratcheted ribosome.,Kumar V, Chen Y, Ero R, Ahmed T, Tan J, Li Z, Wong AS, Bhushan S, Gao YG Proc Natl Acad Sci U S A. 2015 Aug 17. pii: 201513216. PMID:26283392<ref>PMID:26283392</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 09:39, 2 September 2015
Structure of ppGpp BipAStructure of ppGpp BipA
Structural highlights
Publication Abstract from PubMedBPI-inducible protein A (BipA) is a member of the family of ribosome-dependent translational GTPase (trGTPase) factors along with elongation factors G and 4 (EF-G and EF4). Despite being highly conserved in bacteria and playing a critical role in coordinating cellular responses to environmental changes, its structures (isolated and ribosome bound) remain elusive. Here, we present the crystal structures of apo form and GTP analog, GDP, and guanosine-3',5'-bisdiphosphate (ppGpp)-bound BipA. In addition to having a distinctive domain arrangement, the C-terminal domain of BipA has a unique fold. Furthermore, we report the cryo-electron microscopy structure of BipA bound to the ribosome in its active GTP form and elucidate the unique structural attributes of BipA interactions with the ribosome and A-site tRNA in the light of its possible function in regulating translation. Structure of BipA in GTP form bound to the ratcheted ribosome.,Kumar V, Chen Y, Ero R, Ahmed T, Tan J, Li Z, Wong AS, Bhushan S, Gao YG Proc Natl Acad Sci U S A. 2015 Aug 17. pii: 201513216. PMID:26283392[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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