2v9v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==Overview==
-
The crystal structure of the first two winged-helix motifs of translation, elongation factor SelB from Moorella thermoacetica has been determined at, 1.1 A resolution. Compared with the previous structure of the two domains, in conjunction with winged-helix modules 3 and 4, the first winged-helix, domain underwent a substantial conformational change during which the, alpha-helical and beta-sheet portions of the element opened up like a, shell. This conformational rearrangement was elicited by a change in the, orientation of Trp396, leading to the disclosure of a bona fide, ligand-binding site in the direct vicinity of Trp396. Additionally, the, C-terminal tail of the second domain followed a different path compared, with the previous structure. It is conceivable that these conformational, switches constitute part of the molecular mechanism that underlies the, communication between the N-terminal part of SelB, which binds, Sec-tRNA(Sec) and GTP, and the C-terminal part of the protein, which binds, selenocysteine-insertion sequences.
+
The crystal structure of the first two winged-helix motifs of translation elongation factor SelB from Moorella thermoacetica has been determined at 1.1 A resolution. Compared with the previous structure of the two domains in conjunction with winged-helix modules 3 and 4, the first winged-helix domain underwent a substantial conformational change during which the alpha-helical and beta-sheet portions of the element opened up like a shell. This conformational rearrangement was elicited by a change in the orientation of Trp396, leading to the disclosure of a bona fide ligand-binding site in the direct vicinity of Trp396. Additionally, the C-terminal tail of the second domain followed a different path compared with the previous structure. It is conceivable that these conformational switches constitute part of the molecular mechanism that underlies the communication between the N-terminal part of SelB, which binds Sec-tRNA(Sec) and GTP, and the C-terminal part of the protein, which binds selenocysteine-insertion sequences.
==About this Structure==
==About this Structure==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ganichkin, O.]]
[[Category: Ganichkin, O.]]
-
[[Category: Wahl, M.C.]]
+
[[Category: Wahl, M C.]]
[[Category: CL]]
[[Category: CL]]
[[Category: NA]]
[[Category: NA]]
Line 28: Line 28:
[[Category: winged-helix domain]]
[[Category: winged-helix domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:50:44 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:54:29 2008''

Revision as of 16:54, 21 February 2008


2v9v, resolution 1.10Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF MOORELLA THERMOACETICA SELB(377-511)

Overview

The crystal structure of the first two winged-helix motifs of translation elongation factor SelB from Moorella thermoacetica has been determined at 1.1 A resolution. Compared with the previous structure of the two domains in conjunction with winged-helix modules 3 and 4, the first winged-helix domain underwent a substantial conformational change during which the alpha-helical and beta-sheet portions of the element opened up like a shell. This conformational rearrangement was elicited by a change in the orientation of Trp396, leading to the disclosure of a bona fide ligand-binding site in the direct vicinity of Trp396. Additionally, the C-terminal tail of the second domain followed a different path compared with the previous structure. It is conceivable that these conformational switches constitute part of the molecular mechanism that underlies the communication between the N-terminal part of SelB, which binds Sec-tRNA(Sec) and GTP, and the C-terminal part of the protein, which binds selenocysteine-insertion sequences.

About this Structure

2V9V is a Single protein structure of sequence from Moorella thermoacetica with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Conformational switches in winged-helix domains 1 and 2 of bacterial translation elongation factor SelB., Ganichkin O, Wahl MC, Acta Crystallogr D Biol Crystallogr. 2007 Oct;63(Pt 10):1075-81. Epub 2007, Sep 19. PMID:17881825

Page seeded by OCA on Thu Feb 21 18:54:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools