This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2f7t
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2f7t.gif|left|200px]] | [[Image:2f7t.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2f7t", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_2f7t| PDB=2f7t | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Crystal structure of the catalytic domain of Mos1 mariner transposase''' | '''Crystal structure of the catalytic domain of Mos1 mariner transposase''' | ||
| Line 30: | Line 27: | ||
[[Category: Taylor, P.]] | [[Category: Taylor, P.]] | ||
[[Category: Walkinshaw, M D.]] | [[Category: Walkinshaw, M D.]] | ||
| - | [[Category: | + | [[Category: Ddd motif]] |
| - | [[Category: | + | [[Category: Rnase-h like fold]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:33:51 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:33, 4 May 2008
Crystal structure of the catalytic domain of Mos1 mariner transposase
Overview
We present the crystal structure of the catalytic domain of Mos1 transposase, a member of the Tc1/mariner family of transposases. The structure comprises an RNase H-like core, bringing together an aspartic acid triad to form the active site, capped by N- and C-terminal alpha-helices. We have solved structures with either one Mg2+ or two Mn2+ ions in the active site, consistent with a two-metal mechanism for catalysis. The lack of hairpin-stabilizing structural motifs is consistent with the absence of a hairpin intermediate in Mos1 excision. We have built a model for the DNA-binding domain of Mos1 transposase, based on the structure of the bipartite DNA-binding domain of Tc3 transposase. Combining this with the crystal structure of the catalytic domain provides a model for the paired-end complex formed between a dimer of Mos1 transposase and inverted repeat DNA. The implications for the mechanisms of first and second strand cleavage are discussed.
About this Structure
2F7T is a Single protein structure of sequence from Drosophila mauritiana. Full crystallographic information is available from OCA.
Reference
Mechanism of Mos1 transposition: insights from structural analysis., Richardson JM, Dawson A, O'Hagan N, Taylor P, Finnegan DJ, Walkinshaw MD, EMBO J. 2006 Mar 22;25(6):1324-34. Epub 2006 Mar 2. PMID:16511570 Page seeded by OCA on Sun May 4 03:33:51 2008
