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'''Crystal Structure of Domain Swapped trp Aporepressor in 30%(v/v) Isopropanol''' | '''Crystal Structure of Domain Swapped trp Aporepressor in 30%(v/v) Isopropanol''' | ||
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[[Category: Carey, J.]] | [[Category: Carey, J.]] | ||
[[Category: Lawson, C L.]] | [[Category: Lawson, C L.]] | ||
[[Category: | [[Category: Alcohol induced conformational rearrangement]] | ||
[[Category: | [[Category: Dna binding protein]] | ||
[[Category: | [[Category: Domain swapping]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:05:59 2008'' | |||
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Revision as of 22:06, 2 May 2008
Crystal Structure of Domain Swapped trp Aporepressor in 30%(v/v) Isopropanol
Overview
The E. coli trp repressor (trpR) homodimer recognizes its palindromic DNA binding site through a pair of flexible helix-turn-helix (HTH) motifs displayed on an intertwined helical core. Flexible N-terminal arms mediate association between dimers bound to tandem DNA sites. The 2.5 A X-ray structure of trpR crystallized in 30% (v/v) isopropanol reveals a substantial conformational rearrangement of HTH motifs and N-terminal arms, with the protein appearing in the unusual form of an ordered 3D domain-swapped supramolecular array. Small angle X-ray scattering measurements show that the self-association properties of trpR in solution are fundamentally altered by isopropanol.
About this Structure
1MI7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
E. coli trp repressor forms a domain-swapped array in aqueous alcohol., Lawson CL, Benoff B, Berger T, Berman HM, Carey J, Structure. 2004 Jun;12(6):1099-108. PMID:15274929 Page seeded by OCA on Sat May 3 01:05:59 2008
