5a9y: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5a9y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A9Y FirstGlance]. <br>
<table><tr><td colspan='2'>[[5a9y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A9Y FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G4P:GUANOSINE-5,3-TETRAPHOSPHATE'>G4P</scene></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]] 4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G4P:GUANOSINE-5,3-TETRAPHOSPHATE'>G4P</scene></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=5a9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a9y OCA], [https://pdbe.org/5a9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a9y RCSB], [https://www.ebi.ac.uk/pdbsum/5a9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a9y ProSAT]</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=5a9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a9y OCA], [https://pdbe.org/5a9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a9y RCSB], [https://www.ebi.ac.uk/pdbsum/5a9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a9y ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/BIPA_ECO27 BIPA_ECO27] A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA (By similarity). GTPase that impacts interactions between enteropathogenic E.coli (EPEC) and epithelial cells and also has an effect on motility (PubMed:9622352).[HAMAP-Rule:MF_00849]<ref>PMID:9622352</ref>  
[https://www.uniprot.org/uniprot/BIPA_ECO27 BIPA_ECO27] A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA (By similarity). GTPase that impacts interactions between enteropathogenic E.coli (EPEC) and epithelial cells and also has an effect on motility (PubMed:9622352).[HAMAP-Rule:MF_00849]<ref>PMID:9622352</ref>  
<div style="background-color:#fffaf0;">
== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5a9y" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==

Latest revision as of 10:21, 1 May 2024

Structure of ppGpp BipAStructure of ppGpp BipA

Structural highlights

5a9y is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BIPA_ECO27 A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA (By similarity). GTPase that impacts interactions between enteropathogenic E.coli (EPEC) and epithelial cells and also has an effect on motility (PubMed:9622352).[HAMAP-Rule:MF_00849][1]

See Also

References

  1. ↑ Farris M, Grant A, Richardson TB, O'Connor CD. BipA: a tyrosine-phosphorylated GTPase that mediates interactions between enteropathogenic Escherichia coli (EPEC) and epithelial cells. Mol Microbiol. 1998 Apr;28(2):265-79. PMID:9622352 doi:10.1046/j.1365-2958.1998.00793.x

5a9y, resolution 4.00Å

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