1GH8

SOLUTION STRUCTURE OF THE ARCHAEAL TRANSLATION ELONGATION FACTOR 1BETA FROM METHANOBACTERIUM THERMOAUTOTROPHICUM

Replaces:  1D5K

Summary for 1GH8

• Entry DOI: 10.2210/pdb1gh8/pdb
• Descriptor: TRANSLATION ELONGATION FACTOR 1BETA (1 entity in total)
• Functional Keywords: alpha-beta sandwich, gene regulation, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg
• Biological source: Methanothermobacter thermautotrophicus
• Total number of polymer chains: 1
• Total formula weight: 9539.80

Authors

Kozlov, G.,Ekiel, I.,Gehring, K.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2000-11-30, release date: 2000-12-13, Last modification date: 2023-12-27)

Primary citation

Kozlov, G.,Ekiel, I.,Beglova, N.,Yee, A.,Dharamsi, A.,Engel, A.,Siddiqui, N.,Nong, A.,Gehring, K.
Rapid fold and structure determination of the archaeal translation elongation factor 1beta from Methanobacterium thermoautotrophicum.
J.Biomol.NMR, 17:187-194, 2000

PubMed Abstract: The tertiary fold of the elongation factor, aEF-1beta, from Methanobacterium thermoautotrophicum was determined in a high-throughput fashion using a minimal set of NMR experiments. NMR secondary structure prediction, deuterium exchange experiments and the analysis of chemical shift perturbations were combined to identify the protein fold as an alpha-beta sandwich typical of many RNA binding proteins including EF-G. Following resolution of the tertiary fold, a high resolution structure of aEF-1beta was determined using heteronuclear and homonuclear NMR experiments and a semi-automated NOESY assignment strategy. Analysis of the aEF-1beta structure revealed close similarity to its human analogue, eEF-1beta. In agreement with studies on EF-Ts and human EF-1beta, a functional mechanism for nucleotide exchange is proposed wherein Phe46 on an exposed loop acts as a lever to eject GDP from the associated elongation factor G-protein, aEF-1alpha. aEF-1beta was also found to bind calcium in the groove between helix alpha2 and strand beta4. This novel feature was not observed previously and may serve a structural function related to protein stability or may play a functional role in archaeal protein translation.

PubMed: 10959626
DOI: 10.1023/A:1008363304977

Experimental method

SOLUTION NMR