From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1e52.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1e52.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1e52| PDB=1e52 | SCENE= }} | | {{STRUCTURE_1e52| PDB=1e52 | SCENE= }} |
| | | | |
| - | '''SOLUTION STRUCTURE OF ESCHERICHIA COLI UVRB C-TERMINAL DOMAIN'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11697728}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11697728 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_11697728}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| - | 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]. | + | 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== |
| Line 32: |
Line 36: |
| | [[Category: Uvrb]] | | [[Category: Uvrb]] |
| | [[Category: Uvrc binding domain]] | | [[Category: Uvrc binding domain]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:40:23 2008'' | + | |
| | + | ''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
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
