Protein Family Models

This entry represents a beta-barrel domain that is found C-terminal in homologues of elongation factor eEF1A. Paper describing PDB structure 1f60. [1]. 11106763. Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha. Andersen GR, Pedersen L, Valente L, Chatterjee I, Kinzy TG, Kjeldgaard M, Nyborg J;. Mol Cell. 2000;6:1261-1266. Paper describing PDB structure 1jny. [2]. 11574461. The crystal structure of Sulfolobus solfataricus elongation factor 1alpha in complex with GDP reveals novel features in nucleotide binding and exchange. Vitagliano L, Masullo M, Sica F, Zagari A, Bocchini V;. EMBO J. 2001;20:5305-5311. Paper describing PDB structure 1r5b. [3]. 15099522. Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe. Kong C, Ito K, Walsh MA, Wada M, Liu Y, Kumar S, Barford D, Nakamura Y, Song H;. Mol Cell. 2004;14:233-245. Paper describing PDB structure 1zun. [4]. 16387658. Molecular basis for G protein control of the prokaryotic ATP sulfurylase. Mougous JD, Lee DH, Hubbard SC, Schelle MW, Vocadlo DJ, Berger JM, Bertozzi CR;. Mol Cell. 2006;21:109-122. Paper describing PDB structure 3e1y. [5]. 19417105. Structural insights into eRF3 and stop codon recognition by eRF1. Cheng Z, Saito K, Pisarev AV, Wada M, Pisareva VP, Pestova TV, Gajda M, Round A, Kong C, Lim M, Nakamura Y, Svergun DI, Ito K, Song H;. Genes Dev. 2009;23:1106-1118. (from Pfam)

Date:

2024-10-29

Elongation factor Tu consists of several structural domains, and this is usually the fourth. (from Pfam)

Date:

2024-08-14

Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to Pfam:PF03143, and in fact has weak sequence matches to this domain. [1]. 7491491. Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Reshetnikova L, Clark BF, Nyborg J;. Science 1995;270:1464-1472. (from Pfam)

Date:

2024-10-16

Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA [1] and binding to EF-Ts Pfam:PF00889 [2]. [1]. 7491491. Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Reshetnikova L, Clark BF, Nyborg J;. Science 1995;270:1464-1472. [2]. 9253415. Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus. Wang Y, Jiang Y, Meyering-Voss M, Sprinzl M, Sigler PB;. Nat Struct Biol 1997;4:650-656. (from Pfam)

Date:

2024-10-16

This domain contains a P-loop motif, also found in several other families such as Pfam:PF00071, Pfam:PF00025 and Pfam:PF00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains. Cryoelectron microscopy structure. [1]. 9311785. Visualization of elongation factor Tu on the Escherichia coli ribosome. Stark H, Rodnina MV, Rinke-Appel J, Brimacombe R, Wintermeyer W, van Heel M;. Nature 1997;389:403-406. (from Pfam)

Date:

2024-10-16

translation elongation factor EF1A (EF1-alpha) family protein similar to Homo sapiens eukaryotic peptide chain release factor GTP-binding subunit ERF3A that is involved in translation termination in response to the termination codons UAA, UAG and UGA

Date:

2020-12-11

EF-1-alpha; EF-Tu; promotes GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis; when the tRNA anticodon matches the mRNA codon, GTP hydrolysis results; the inactive EF-1-alpha-GDP leaves the ribosome and GDP/GTP exchange is promoted by EF-1-beta

Date:

2020-10-26

This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels.

Gene:

tuf

Date:

2024-05-30