1gh8
SOLUTION STRUCTURE OF THE ARCHAEAL TRANSLATION ELONGATION FACTOR 1BETA FROM METHANOBACTERIUM THERMOAUTOTROPHICUM
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OverviewOverview
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.
About this StructureAbout this Structure
1GH8 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. This structure superseeds the now removed PDB entry 1D5K. Full crystallographic information is available from OCA.
ReferenceReference
Rapid fold and structure determination of the archaeal translation elongation factor 1beta from Methanobacterium thermoautotrophicum., Kozlov G, Ekiel I, Beglova N, Yee A, Dharamsi A, Engel A, Siddiqui N, Nong A, Gehring K, J Biomol NMR. 2000 Jul;17(3):187-94. PMID:10959626
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