1qyn
From Proteopedia
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Crystal Structure of SecB from Escherichia coli
Overview
The chaperone SecB from Escherichia coli is primarily involved in passing, precursor proteins into the Sec system via specific interactions with, SecA. The crystal structure of SecB from E. coli has been solved to 2.35 A, resolution. The structure shows flexibility in the crossover loop and the, helix-connecting loop, regions that have been implicated to be part of the, SecB substrate-binding site. Moreover conformational variability of Trp36, is observed as well as different loop conformations for the different, monomers. Based on this, we speculate that SecB can regulate the access or, extent of its hydrophobic substrate-binding site, by modulating the, conformation of the crossover loop and the helix-connecting loop. The, structure also clearly explains why the tetrameric equilibrium is shifted, towards the dimeric state in the mutant SecBCys76Tyr. The buried cysteine, residue is crucial for tight packing, and mutations are likely to disrupt, the tetramer formation but not the dimer formation.
About this Structure
1QYN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of SecB from Escherichia coli., Dekker C, de Kruijff B, Gros P, J Struct Biol. 2003 Dec;144(3):313-9. PMID:14643199
Page seeded by OCA on Wed Nov 21 01:07:38 2007
