1byk
From Proteopedia
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| - | [[Image:1byk.jpg|left|200px]] | + | [[Image:1byk.jpg|left|200px]] |
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| - | '''TREHALOSE REPRESSOR FROM ESCHERICHIA COLI''' | + | {{Structure |
| + | |PDB= 1byk |SIZE=350|CAPTION= <scene name='initialview01'>1byk</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=T6P:TREHALOSE-6-PHOSPHATE'>T6P</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''TREHALOSE REPRESSOR FROM ESCHERICHIA COLI''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BYK is a [ | + | 1BYK 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=1BYK OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose., Hars U, Horlacher R, Boos W, Welte W, Diederichs K, Protein Sci. 1998 Dec;7(12):2511-21. PMID:[http:// | + | Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose., Hars U, Horlacher R, Boos W, Welte W, Diederichs K, Protein Sci. 1998 Dec;7(12):2511-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9865945 9865945] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: trehalose repressor]] | [[Category: trehalose repressor]] | ||
| - | ''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 10:17:30 2008'' |
Revision as of 08:17, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
TREHALOSE REPRESSOR FROM ESCHERICHIA COLI
Overview
The crystal structure of the Escherichia coli trehalose repressor (TreR) in a complex with its inducer trehalose-6-phosphate was determined by the method of multiple isomorphous replacement (MIR) at 2.5 A resolution, followed by the structure determination of TreR in a complex with its noninducer trehalose at 3.1 A resolution. The model consists of residues 61 to 315 comprising the effector binding domain, which forms a dimer as in other members of the LacI family. This domain is composed of two similar subdomains each consisting of a central beta-sheet sandwiched between alpha-helices. The effector binding pocket is at the interface of these subdomains. In spite of different physiological functions, the crystal structures of the two complexes of TreR turned out to be virtually identical to each other with the conformation being similar to those of the effector binding domains of the LacI and PurR in complex with their effector molecules. According to the crystal structure, the noninducer trehalose binds to a similar site as the trehalose portion of trehalose-6-phosphate. The binding affinity for the former is lower than for the latter. The noninducer trehalose thus binds competitively to the repressor. Unlike the phosphorylated inducer molecule, it is incapable of blocking the binding of the repressor headpiece to its operator DNA. The ratio of the concentrations of trehalose-6-phosphate and trehalose thus is used to switch between the two alternative metabolic uses of trehalose as an osmoprotectant and as a carbon source.
About this Structure
1BYK is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose., Hars U, Horlacher R, Boos W, Welte W, Diederichs K, Protein Sci. 1998 Dec;7(12):2511-21. PMID:9865945
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