1mi7: Difference between revisions

Revision as of 00:01, 3 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1mi7.png

Template:STRUCTURE 1mi7

Crystal Structure of Domain Swapped trp Aporepressor in 30%(v/v) IsopropanolCrystal Structure of Domain Swapped trp Aporepressor in 30%(v/v) Isopropanol

Template:ABSTRACT PUBMED 15274929

About this StructureAbout this Structure

1MI7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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 Thu Jul 3 00:01:49 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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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===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15274929}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15274929}}
 ==About this Structure==
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 [[Category: Dna binding protein]]
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