2bsk: Difference between revisions
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|PDB= 2bsk |SIZE=350|CAPTION= <scene name='initialview01'>2bsk</scene>, resolution 3.3Å | |PDB= 2bsk |SIZE=350|CAPTION= <scene name='initialview01'>2bsk</scene>, resolution 3.3Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bsk OCA], [http://www.ebi.ac.uk/pdbsum/2bsk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bsk RCSB]</span> | |||
}} | }} | ||
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[[Category: Ryan, M T.]] | [[Category: Ryan, M T.]] | ||
[[Category: Webb, C T.]] | [[Category: Webb, C T.]] | ||
[[Category: protein transport]] | [[Category: protein transport]] | ||
[[Category: tim complex | [[Category: tim9,tim10,mitochondrial protein import,tim complex]] | ||
''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 02:11:10 2008'' | ||
Revision as of 02:11, 31 March 2008
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| , resolution 3.3Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE TIM9 TIM10 HEXAMERIC COMPLEX
OverviewOverview
Import of proteins into mitochondria occurs by coordinated actions of preprotein translocases in the outer and inner membranes. Tim9 and Tim10 are translocase components of the intermembrane space, related to deafness-dystonia peptide 1 (DDP1). They coassemble into a hexamer, TIM9.10, which captures and chaperones precursors of inner membrane metabolite carriers as they exit the TOM channel in the outer membrane. The crystal structure of TIM9.10 reveals a previously undescribed alpha-propeller topology in which helical "blades" radiate from a narrow central pore lined with polar residues. The propeller blades are reminiscent of "tentacles" in chaperones Skp and prefoldin. In each TIM9.10 subunit, a signature "twin CX3C" motif forms two intramolecular disulfides. There is no obvious binding pocket for precursors, which we suggest employ the chaperone-like tentacles of TIM9.10 as surrogate lipid contacts. The first reported crystal structure of a mitochondrial translocase assembly provides insights into selectivity and regulation of precursor import.
About this StructureAbout this Structure
2BSK is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller., Webb CT, Gorman MA, Lazarou M, Ryan MT, Gulbis JM, Mol Cell. 2006 Jan 6;21(1):123-33. PMID:16387659
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