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1e52

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{{STRUCTURE_1e52| PDB=1e52 | SCENE= }}
{{STRUCTURE_1e52| PDB=1e52 | SCENE= }}
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'''SOLUTION STRUCTURE OF ESCHERICHIA COLI UVRB C-TERMINAL DOMAIN'''
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===SOLUTION STRUCTURE OF ESCHERICHIA COLI UVRB C-TERMINAL DOMAIN===
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==Overview==
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The solution structure, thermodynamic stability and hydrodynamic properties of the 55-residue C-terminal domain of UvrB that interacts with UvrC during excision repair in E. coli have been determined using a combination of high resolution NMR, ultracentrifugation, 15N NMR relaxation, gel permeation, NMR diffusion, circular dichroism and differential scanning calorimetry. The subunit molecular weight is 7,438 kDa., compared with 14.5+/-1.0 kDa. determined by equilibrium sedimentation, indicating a dimeric structure. The structure determined from NMR showed a stable dimer of anti-parallel helical hairpins that associate in an unusual manner, with a small and hydrophobic interface. The Stokes radius of the protein decreases from a high plateau value (ca. 22 A) at protein concentrations greater than 4 microM to about 18 A at concentrations less than 0.1 microM. The concentration and temperature-dependence of the far UV circular dichroism show that the protein is thermally stable (Tm ca. 71.5 degrees C at 36 microM). The simplest model consistent with these data was a dimer dissociating into folded monomers that then unfolds co-operatively. The van't Hoff enthalpy and dissociation constant for both transition was derived by fitting, with deltaH1=23 kJ mol(-1). K1(298)=0.4 microM and deltaH2= 184 kJ mol(-1). This is in good agreement with direct calorimetric analysis of the thermal unfolding of the protein, which gave a calorimetric enthalpy change of 181 kJ mol(-1) and a van't Hoff enthalpy change of 354 kJ mol(-1), confirming the dimer to monomer unfolding. The thermodynamic data can be reconciled with the observed mode of dimerisation. 15N NMR relaxation measurements at 14.1 T and 11.75 T confirmed that the protein behaves as an asymmetric dimer at mM concentrations, with a flexible N-terminal linker for attachment to the remainder of the UvrB protein. The role of dimerisation of this domain in the excision repair mechanism is discussed.
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(as it appears on PubMed at http://www.pubmed.gov), where 11697728 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11697728}}
==About this Structure==
==About this Structure==
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1E52 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=1E52 OCA].
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1E52 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E52 OCA].
==Reference==
==Reference==
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[[Category: Uvrb]]
[[Category: Uvrb]]
[[Category: Uvrc binding domain]]
[[Category: Uvrc binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:40:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:09:43 2008''

Revision as of 21:09, 30 June 2008

Image:1e52.png

Template:STRUCTURE 1e52

SOLUTION STRUCTURE OF ESCHERICHIA COLI UVRB C-TERMINAL DOMAIN

Template:ABSTRACT PUBMED 11697728

About this Structure

1E52 is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

Solution structure, hydrodynamics and thermodynamics of the UvrB C-terminal domain., Alexandrovich A, Czisch M, Frenkiel TA, Kelly GP, Goosen N, Moolenaar GF, Chowdhry BZ, Sanderson MR, Lane AN, J Biomol Struct Dyn. 2001 Oct;19(2):219-36. PMID:11697728

Page seeded by OCA on Tue Jul 1 00:09:43 2008

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