2f5g
From Proteopedia
(New page: 200px<br /><applet load="2f5g" size="350" color="white" frame="true" align="right" spinBox="true" caption="2f5g, resolution 1.70Å" /> '''Crystal structure of...) |
|||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | IS200 transposases, present in many bacteria and Archaea, appear to be | + | 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. |
==About this Structure== | ==About this Structure== | ||
| Line 13: | Line 13: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sulfolobus solfataricus]] | [[Category: Sulfolobus solfataricus]] | ||
| - | [[Category: Kang, J | + | [[Category: Kang, J Y.]] |
| - | [[Category: Kim, D | + | [[Category: Kim, D J.]] |
| - | [[Category: Kim, H | + | [[Category: Kim, H S.]] |
| - | [[Category: Kim, K | + | [[Category: Kim, K H.]] |
| - | [[Category: Lee, H | + | [[Category: Lee, H H.]] |
| - | [[Category: Suh, S | + | [[Category: Suh, S W.]] |
| - | [[Category: Yoon, J | + | [[Category: Yoon, J Y.]] |
[[Category: dimer]] | [[Category: dimer]] | ||
[[Category: stem-loop binding]] | [[Category: stem-loop binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:17:56 2008'' |
Revision as of 15:17, 21 February 2008
|
Crystal structure of IS200 transposase
Overview
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.
About this Structure
2F5G is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 17:17:56 2008
