D
IPR053905

Elongation factor G-like, domain II

InterPro entry
Short nameEF-G-like_DII
Overlapping
homologous
superfamilies
 
domain relationships

Description

This entry represents a domain found in the bacterial group of Elongation factor G (EF-G) proteins, which catalyse the translocation step of translation. It consists of five structural domains, this entry represents the second domain
[1]
which adopts a β-barrel structure. This entry also includes other translation factors such as translation initiation factor IF-2, peptide chain release factor 3 (RF3), mitochondrial ribosome-releasing factor 2 (also known as EFG2 mitochondrial)
[2, 3]
, among others.

References

1.The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. al-Karadaghi S, Aevarsson A, Garber M, Zheltonosova J, Liljas A. Structure 4, 555-65, (1996). View articlePMID: 8736554

2.Structural basis of translation termination, rescue, and recycling in mammalian mitochondria. Kummer E, Schubert KN, Schoenhut T, Scaiola A, Ban N. Mol Cell 81, 2566-2582.e6, (2021). View articlePMID: 33878294

3.Distinct mechanisms of the human mitoribosome recycling and antibiotic resistance. Koripella RK, Deep A, Agrawal EK, Keshavan P, Banavali NK, Agrawal RK. Nat Commun 12, 3607, (2021). View articlePMID: 34127662

Further reading

4. Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D, Liljas A. J. Mol. Biol. 303, 593-603, (2000). View articlePMID: 11054294

5. X-Ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding. Roll-Mecak A, Cao C, Dever TE, Burley SK. Cell 103, 781-92, (2000). View articlePMID: 11114334

6. The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution. Czworkowski J, Wang J, Steitz TA, Moore PB. EMBO J. 13, 3661-8, (1994). View articlePMID: 8070396

Cross References

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