Virtuelle (Nano) Welten PDB Molecule of the Month 82: Elongation Factors

Structure ID	Title	Authors	Publication Year	Journal Name	Volume ID	First Page	Pubmed
1AIP	Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus.	Wang, Y., Jiang, Y., Meyering-Voss, M., Sprinzl, M., Sigler, P.B.	1997	Nat.Struct.Biol.	4	650	9253415
1EFU	The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution.	Kawashima, T., Berthet-Colominas, C., Wulff, M., Cusack, S., Leberman, R.	1996	Nature	379	511	8596629
1ELO	Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.	AEvarsson, A., Brazhnikov, E., Garber, M., Zheltonosova, J., Chirgadze, Y., al-Karadaghi, S., Svensson, L.A., Liljas, A.	1994	EMBO J.	13	3669	8070397
1EO0	Structure of a conserved domain common to the transcription factors TFIIS, elongin A, and CRSP70	Booth, V., Koth, C., Edwards, A.M., Arrowsmith, C.H.	2000	J.Biol.Chem.	275	31266	10811649
1KJZ	The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors.	Schmitt, E., Blanquet, S., Mechulam, Y.	2002	EMBO J.	21	1821	11927566
1KK0	The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors.	Schmitt, E., Blanquet, S., Mechulam, Y.	2002	EMBO J.	21	1821	11927566
1KK1	The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors.	Schmitt, E., Blanquet, S., Mechulam, Y.	2002	EMBO J.	21	1821	11927566
1KK2	The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors.	Schmitt, E., Blanquet, S., Mechulam, Y.	2002	EMBO J.	21	1821	11927566
1KK3	The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors.	Schmitt, E., Blanquet, S., Mechulam, Y.	2002	EMBO J.	21	1821	11927566
1OB5	Enacyloxin Iia Pinpoints a Binding Pocket of Elongation Factor TU for Development of Novel Antibiotics.	Parmeggiani, A., Krab, I.M., Watanabe, T., Nielsen, R.C., Dahlberg, C., Nyborg, J., Nissen, P.	2006	J.Biol.Chem.	281	2893	n/a
1Q93	The common and distinctive features of the bulged-G motif based on a 1.04 A resolution RNA structure	Correll, C.C., Beneken, J., Plantinga, M.J., Lubbers, M., Chan, Y.L.	2003	Nucleic Acids Res.	31	6806	14627814
1Q96	The common and distinctive features of the bulged-G motif based on a 1.04 A resolution RNA structure	Correll, C.C., Beneken, J., Plantinga, M.J., Lubbers, M., Chan, Y.L.	2003	Nucleic Acids Res.	31	6806	14627814
1SKQ	The crystal structure of Sulfolobus solfataricus elongation factor 1alpha in complex with magnesium and GDP.	Vitagliano, L., Ruggiero, A., Masullo, M., Cantiello, P., Arcari, P., Zagari, A.	2004	Biochemistry	43	6630	15157096
1TTT	Crystal Structure of the Ternary Complex of Phe-tRNA(Phe), EF-TU, and a GTP Analog	Nissen, P., Kjeldgaard, M., Thirup, S., Polekhina, G., Reshetnikova, L., Clark, B.F., Nyborg, J.	1995	Science	270	1464	n/a
1TUI	Helix unwinding in the effector region of elongation factor EF-Tu-GDP.	Polekhina, G., Thirup, S., Kjeldgaard, M., Nissen, P., Lippmann, C., Nyborg, J.	1996	Structure	4	1141	8939739
1UON	Reovirus Polymerase Lambda3 Localized by Cryo-Electron Microscopy of Virions at a Resolution of 7.6 A	Zhang, X., Walker, S.B., Chipman, P.R., Nibert, M.L., Baker, T.S.	2003	Nat.Struct.Mol.Biol.	10	1011	n/a
1WB1	Selenocysteine tRNA-Specific Elongation Factor Selb is a Structural Chimaera of Elongation and Initiation Factors	Leibundgut, M., Frick, C., Thanbichler, M., Boeck, A., Ban, N.	2004	Embo J.	n/a	n/a	n/a
1WB2	Selenocysteine tRNA-Specific Elongation Factor Selb is a Structural Chimaera of Elongation and Initiation Factors	Leibundgut, M., Frick, C., Thanbichler, M., Boeck, A., Ban, N.	2004	Embo J.	n/a	n/a	n/a
1WB3	Selenocysteine tRNA-Specific Elongation Factor Selb is a Structural Chimaera of Elongation and Initiation Factors	Leibundgut, M., Frick, C., Thanbichler, M., Boeck, A., Ban, N.	2004	Embo J.	n/a	n/a	n/a
1XB2	Crystal Structure of the Bovine Mitochondrial Elongation Factor Tu.Ts Complex	Jeppesen, M.G., Navratil, T., Spremulli, L.L., Nyborg, J.	2005	J.Biol.Chem.	280	5071	15557323
2BM0	Structural Insights Into Fusidic Acid Resistance and Sensitivity in EF-G	Hansson, S., Singh, R., Gudkov, A.T., Liljas, A., Logan, D.T.	2005	J.Mol.Biol.	348	939	n/a
2BM1	Structural Insights Into Fusidic Acid Resistance and Sensitivity in EF-G	Hansson, S., Singh, R., Gudkov, A.T., Liljas, A., Logan, D.T.	2005	J.Mol.Biol.	348	939	n/a
2BV3	Crystal Structure of a Mutant Elongation Factor G Trapped with a GTP Analogue.	Hansson, S., Singh, R., Gudkov, A.T., Liljas, A., Logan, D.T.	n/a	To be Published	n/a	n/a	n/a
2FX3	Solving the structure of Escherichia coli elongation factor Tu using a twinned data set.	Heffron, S.E., Moeller, R., Jurnak, F.	2006	ACTA CRYSTALLOGR.,SECT.D	62	433	16552145
430D	Crystal structure of the ribosomal RNA domain essential for binding elongation factors.	Correll, C.C., Munishkin, A., Chan, Y.L., Ren, Z., Wool, I.G., Steitz, T.A.	1998	Proc.Natl.Acad.Sci.USA	95	13436	9811818
480D	The two faces of the Escherichia coli 23 S rRNA sarcin/ricin domain: the structure at 1.11 A resolution.	Correll, C.C., Wool, I.G., Munishkin, A.	1999	J.Mol.Biol.	292	275	10493875
483D	The two faces of the Escherichia coli 23 S rRNA sarcin/ricin domain: the structure at 1.11 A resolution.	Correll, C.C., Wool, I.G., Munishkin, A.	1999	J.Mol.Biol.	292	275	10493875