1qyn
From Proteopedia
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| - | [[Image:1qyn.gif|left|200px]] | + | [[Image:1qyn.gif|left|200px]] |
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| - | '''Crystal Structure of SecB from Escherichia coli''' | + | {{Structure |
| + | |PDB= 1qyn |SIZE=350|CAPTION= <scene name='initialview01'>1qyn</scene>, resolution 2.35Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= SECB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of SecB from Escherichia coli''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QYN is a [ | + | 1QYN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QYN OCA]. |
==Reference== | ==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:[http:// | + | Crystal structure of SecB from Escherichia coli., Dekker C, de Kruijff B, Gros P, J Struct Biol. 2003 Dec;144(3):313-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14643199 14643199] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tetramer]] | [[Category: tetramer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:44:30 2008'' |
Revision as of 11:44, 20 March 2008
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| , resolution 2.35Å | |||||||
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| Gene: | SECB (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 13:44:30 2008
