2v9v
From Proteopedia
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|PDB= 2v9v |SIZE=350|CAPTION= <scene name='initialview01'>2v9v</scene>, resolution 1.10Å | |PDB= 2v9v |SIZE=350|CAPTION= <scene name='initialview01'>2v9v</scene>, resolution 1.10Å | ||
|SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1lva|1LVA]], [[1wsu|1WSU]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v9v OCA], [http://www.ebi.ac.uk/pdbsum/2v9v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v9v RCSB]</span> | ||
}} | }} | ||
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[[Category: Ganichkin, O.]] | [[Category: Ganichkin, O.]] | ||
[[Category: Wahl, M C.]] | [[Category: Wahl, M C.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: NA]] | ||
[[Category: cytoplasm]] | [[Category: cytoplasm]] | ||
[[Category: gtp-binding]] | [[Category: gtp-binding]] | ||
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[[Category: winged-helix domain]] | [[Category: winged-helix domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:10:05 2008'' |
Revision as of 02:10, 31 March 2008
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| , resolution 1.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Related: | 1LVA, 1WSU
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mon Mar 31 05:10:05 2008
Categories: Moorella thermoacetica | Single protein | Ganichkin, O. | Wahl, M C. | Cytoplasm | Gtp-binding | Nucleotide-binding | Protein biosynthesis | Protein conformational change | Protein dynamic | Selenocysteine | Selenoprotein biosynthesis | Transcription elongation factor selb | Winged-helix domain
