1e52
From Proteopedia
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| - | [[Image:1e52.gif|left|200px]] | + | [[Image:1e52.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF ESCHERICHIA COLI UVRB C-TERMINAL DOMAIN''' | + | {{Structure |
| + | |PDB= 1e52 |SIZE=350|CAPTION= <scene name='initialview01'>1e52</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= UVRB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''SOLUTION STRUCTURE OF ESCHERICHIA COLI UVRB C-TERMINAL DOMAIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E52 is a [ | + | 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]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11697728 11697728] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: uvrc binding domain]] | [[Category: uvrc binding domain]] | ||
| - | ''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 10:49:51 2008'' |
Revision as of 08:49, 20 March 2008
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| Gene: | UVRB (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF ESCHERICHIA COLI UVRB C-TERMINAL DOMAIN
Overview
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.
About this Structure
1E52 is a Single protein structure of sequence from Escherichia coli. Full crystallographic 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
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