2f4f

Crystal structure of IS200 transposase

spinqualitylabelsall models 2f4f, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2f4f is a 2 chain structure with sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MN Related: 2f5g Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed IS200 transposases, present in many bacteria and Archaea, appear to be distinct from other groups of transposases. To provide a structural basis for understanding the action of IS200 transposases, we have determined the crystal structure of the SSO1474 protein from Sulfolobus solfataricus, a member of the IS200 family, in both Mn(2+)-bound and Mn(2+)-free forms. Its monomer fold is distinct from other classes of structurally characterized transposases. Two monomers form a tight dimer by exchanging the C-terminal alpha-helix and by merging the two central beta-sheets into a large beta-sheet. Glu(55), His(62), and four water molecules provide the direct coordination sphere of the catalytically essential metal ion in the Mn(2+)-bound structure. His(16), Asp(59), and His(60) also play important roles in maintaining the metal binding site. The catalytic site is formed at the interface between monomers. The candidate nucleophile in the transposition mechanism, strictly conserved Tyr(121) coming from the other monomer, is turned away from the active site, suggesting that a conformational change is likely to occur during the catalytic cycle. Crystal structure of a metal ion-bound IS200 transposase.,Lee HH, Yoon JY, Kim HS, Kang JY, Kim KH, Kim DJ, Ha JY, Mikami B, Yoon HJ, Suh SW J Biol Chem. 2006 Feb 17;281(7):4261-6. Epub 2005 Dec 11. PMID:16340015 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA