5fg3 | pdb_00005fg3

Crystal structure of GDP-bound aIF5B from Aeropyrum pernix

spinqualitylabelsall models 5fg3, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fg3 is a 1 chain structure with sequence from Aeropyrum pernix K1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: GDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function IF2P_AERPE Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2 (By similarity). Publication Abstract from PubMed Initiation factor 5B (IF5B) is a universally conserved translational GTPase that catalyzes ribosomal subunit joining. In eukaryotes, IF5B directly interacts via a groove in its domain IV with initiation factor 1A (IF1A), another universally conserved initiation factor, to accomplish efficient subunit joining. Here, we have determined the first structure of a crenarchaeal IF5B, which revealed that the archaea-specific region of IF5B (helix alpha15) binds and occludes the groove of domain IV. Therefore, archaeal IF5B cannot access IF1A in the same manner as eukaryotic IF5B. This fact suggests that different relationships between IF5B and IF1A exist in archaea and eukaryotes. Proteins 2016; 84:712-717. (c) 2016 Wiley Periodicals, Inc. Crystal structure of translation initiation factor 5B from the crenarchaeon Aeropyrum pernix.,Murakami R, Miyoshi T, Uchiumi T, Ito K Proteins. 2016 May;84(5):712-7. doi: 10.1002/prot.25009. Epub 2016 Mar 6. PMID:26868175 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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