1D2E

CRYSTAL STRUCTURE OF MITOCHONDRIAL EF-TU IN COMPLEX WITH GDP

Summary for 1D2E

• Entry DOI: 10.2210/pdb1d2e/pdb
• Related: 1EFC 1TUI
• Descriptor: ELONGATION FACTOR TU (EF-TU), MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: g-protein, beta-barrel, rna binding protein
• Biological source: Bos taurus (cattle)
• Cellular location: Mitochondrion: P49410
• Total number of polymer chains: 4
• Total formula weight: 177035.57

Authors

Andersen, G.R.,Thirup, S.,Spremulli, L.L.,Nyborg, J. (deposition date: 1999-09-23, release date: 1999-09-28, Last modification date: 2024-02-07)

Primary citation

Andersen, G.R.,Thirup, S.,Spremulli, L.L.,Nyborg, J.
High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP.
J.Mol.Biol., 297:421-436, 2000

PubMed Abstract: The crystal structure of bovine mitochondrial elongation factor Tu (EF-Tu) in complex with GDP has been determined at a resolution of 1. 94 A. The structure is similar to that of EF-Tu:GDP from Escherichia coli and Thermus aquaticus, but the orientation of the GDP-binding domain 1 is changed relative to domains 2 and 3. Sixteen conserved water molecules common to EF-Tu and other G-proteins in the GDP-binding site are described. These water molecules create a network linking separated parts of the binding pocket. Mitochondrial EF-Tu binds nucleotides less tightly than prokaryotic EF-Tu possibly due to an increased mobility in regions close to the GDP-binding site. The C-terminal extension of mitochondrial EF-Tu has structural similarities with DNA recognising zinc fingers suggesting that the extension may be involved in recognition of RNA.

PubMed: 10715211
DOI: 10.1006/jmbi.2000.3564

Experimental method

X-RAY DIFFRACTION (1.94 Å)