Elongation factor G-like, domain II
Short name | EF-G-like_DII |
Overlapping homologous superfamilies | |
domain relationships |
Description
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
ENZYME
Contributing Member Database Entry
- Pfam:PF22042