1XB2

Crystal Structure of Bos taurus mitochondrial Elongation Factor Tu/Ts Complex

Summary for 1XB2

• Entry DOI: 10.2210/pdb1xb2/pdb
• Related: 1D2E
• Descriptor: Elongation factor Tu, mitochondrial, Elongation factor Ts, mitochondrial (3 entities in total)
• Functional Keywords: protein-protein complex, translation
• Biological source: Bos taurus (cattle); More
• Cellular location: Mitochondrion: P49410 P43896
• Total number of polymer chains: 2
• Total formula weight: 77508.00

Authors

Jeppesen, M.G.,Navratil, T.,Spremulli, L.L.,Nyborg, J. (deposition date: 2004-08-27, release date: 2004-11-23, Last modification date: 2024-10-16)

Primary citation

Jeppesen, M.G.,Navratil, T.,Spremulli, L.L.,Nyborg, J.
Crystal Structure of the Bovine Mitochondrial Elongation Factor Tu.Ts Complex
J.Biol.Chem., 280:5071-5081, 2005

PubMed Abstract: The three-dimensional structure of the bovine mitochondrial elongation factor (EF)-Tu.Ts complex (EF-Tumt.Tsmt) has been determined to 2.2-A resolution using the multi-wavelength anomalous dispersion experimental method. This complex provides the first insight into the structure of EF-Tsmt. EF-Tsmt is similar to Escherichia coli and Thermus thermophilus EF-Ts in the amino-terminal domain. However, the structure of EF-Tsmt deviates considerably in the core domain with a five-stranded beta-sheet forming a portion of subdomain N of the core. In E. coli EF-Ts, this region is composed of a three-stranded sheet. The coiled-coil domain of the E. coli EF-Ts is largely eroded in EF-Tsmt, in which it consists of a large loop packed against subdomain C of the core. The conformation of bovine EF-Tumt in complex with EF-Tsmt is distinct from its conformation in the EF-Tumt.GDP complex. When domain III of bovine EF-Tumt.GDP is superimposed on domain III of EF-Tumt in the EF-Tumt.Tsmt complex, helix B from domain I is also almost superimposed. However, the rest of domain I is rotated relative to this helix toward domain II, which itself is rotated toward domain I relative to domain III. Extensive contacts are observed between the amino-terminal domain of EF-Tsmt and domain I of EF-Tumt. Furthermore, the conserved TDFV sequence of EF-Tsmt also contacts domain I with the side chain of Asp139 contacting helix B of EF-Tumt and inserting the side chain of Phe140 between helices B and C. The structure of the EF-Tumt.Tsmt complex provides new insights into the nucleotide exchange mechanism and provides a framework for explaining much of the mutational data obtained for this complex.

PubMed: 15557323
DOI: 10.1074/jbc.M411782200

Experimental method

X-RAY DIFFRACTION (2.2 Å)