1la1: Difference between revisions

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[[Image:1la1.gif|left|200px]]<br /><applet load="1la1" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1la1.gif|left|200px]]<br /><applet load="1la1" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1la1, resolution 2.06Å" />

'''Gro-EL Fragment (Apical Domain) Comprising Residues 188-379'''<br />

==Overview==

Advances in understanding how GroEL binds to non-native proteins are, reported. Conformational flexibility in the GroEL apical domain, which, could account for the variety of substrates that GroEL binds, is, illustrated by comparison of several independent crystallographic, structures of apical domain constructs that show conformational plasticity, in helices H and I. Additionally, ESI-MS indicates that apical domain, constructs have co-populated conformations at neutral pH. To assess the, ability of different apical domain conformers to bind co-chaperone and, substrate, model peptides corresponding to the mobile loop of GroES and to, helix D from rhodanese were studied. Analysis of apical domain-peptide, complexes by ESI-MS indicates that only the folded or partially folded, apical domain conformations form complexes that survive gas phase, conditions. Fluorescence binding studies show that the apical domain can, fully bind both peptides independently. No competition for binding was, observed, suggesting the peptides have distinct apical domain-binding, sites. Blocking the GroES-apical domain-binding site in GroEL rendered the, chaperonin inactive in binding GroES and in assisting the folding of, denatured rhodanese, but still capable of binding non-native proteins, supporting the conclusion that GroES and substrate proteins have, at least, partially, distinct binding sites even in the intact GroEL tetradecamer.

Advances in understanding how GroEL binds to non-native proteins are reported. Conformational flexibility in the GroEL apical domain, which could account for the variety of substrates that GroEL binds, is illustrated by comparison of several independent crystallographic structures of apical domain constructs that show conformational plasticity in helices H and I. Additionally, ESI-MS indicates that apical domain constructs have co-populated conformations at neutral pH. To assess the ability of different apical domain conformers to bind co-chaperone and substrate, model peptides corresponding to the mobile loop of GroES and to helix D from rhodanese were studied. Analysis of apical domain-peptide complexes by ESI-MS indicates that only the folded or partially folded apical domain conformations form complexes that survive gas phase conditions. Fluorescence binding studies show that the apical domain can fully bind both peptides independently. No competition for binding was observed, suggesting the peptides have distinct apical domain-binding sites. Blocking the GroES-apical domain-binding site in GroEL rendered the chaperonin inactive in binding GroES and in assisting the folding of denatured rhodanese, but still capable of binding non-native proteins, supporting the conclusion that GroES and substrate proteins have, at least partially, distinct binding sites even in the intact GroEL tetradecamer.

==About this Structure==

1LA1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1LA1 OCA].

1LA1 is a [http://en.wikipedia.org/wiki/Single_protein 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=1LA1 OCA].

==Reference==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Ashcroft, A.E.]]

[[Category: Ashcroft, A E.]]

[[Category: Brinker, A.]]

[[Category: Coyle, J.E.]]

[[Category: Coyle, J E.]]

[[Category: Hartl, U.F.]]

[[Category: Hartl, U F.]]

[[Category: Hayer-Hartl, M.]]

[[Category: Jager, J.]]

[[Category: Kaiser, M.]]

[[Category: Moroder, L.]]

[[Category: Parsons, M.R.]]

[[Category: Parsons, M R.]]

[[Category: Radford, S.E.]]

[[Category: Radford, S E.]]

[[Category: Weber, F.]]

[[Category: molecular chaperone]]

[[Category: protein folding]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 20~~:25:~~06 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:58 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1la1.gif|left|200px]]<br /><applet load="1la1" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1la1.gif|left|200px]]<br /><applet load="1la1" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1la1, resolution 2.06&Aring;" />
 '''Gro-EL Fragment (Apical Domain) Comprising Residues 188-379'''<br />
 ==Overview==
-Advances in understanding how GroEL binds to non-native proteins are, reported. Conformational flexibility in the GroEL apical domain, which, could account for the variety of substrates that GroEL binds, is, illustrated by comparison of several independent crystallographic, structures of apical domain constructs that show conformational plasticity, in helices H and I. Additionally, ESI-MS indicates that apical domain, constructs have co-populated conformations at neutral pH. To assess the, ability of different apical domain conformers to bind co-chaperone and, substrate, model peptides corresponding to the mobile loop of GroES and to, helix D from rhodanese were studied. Analysis of apical domain-peptide, complexes by ESI-MS indicates that only the folded or partially folded, apical domain conformations form complexes that survive gas phase, conditions. Fluorescence binding studies show that the apical domain can, fully bind both peptides independently. No competition for binding was, observed, suggesting the peptides have distinct apical domain-binding, sites. Blocking the GroES-apical domain-binding site in GroEL rendered the, chaperonin inactive in binding GroES and in assisting the folding of, denatured rhodanese, but still capable of binding non-native proteins, supporting the conclusion that GroES and substrate proteins have, at least, partially, distinct binding sites even in the intact GroEL tetradecamer.
+Advances in understanding how GroEL binds to non-native proteins are reported. Conformational flexibility in the GroEL apical domain, which could account for the variety of substrates that GroEL binds, is illustrated by comparison of several independent crystallographic structures of apical domain constructs that show conformational plasticity in helices H and I. Additionally, ESI-MS indicates that apical domain constructs have co-populated conformations at neutral pH. To assess the ability of different apical domain conformers to bind co-chaperone and substrate, model peptides corresponding to the mobile loop of GroES and to helix D from rhodanese were studied. Analysis of apical domain-peptide complexes by ESI-MS indicates that only the folded or partially folded apical domain conformations form complexes that survive gas phase conditions. Fluorescence binding studies show that the apical domain can fully bind both peptides independently. No competition for binding was observed, suggesting the peptides have distinct apical domain-binding sites. Blocking the GroES-apical domain-binding site in GroEL rendered the chaperonin inactive in binding GroES and in assisting the folding of denatured rhodanese, but still capable of binding non-native proteins, supporting the conclusion that GroES and substrate proteins have, at least partially, distinct binding sites even in the intact GroEL tetradecamer.
 ==About this Structure==
-LA1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LA1 OCA].
+LA1 is a [http://en.wikipedia.org/wiki/Single_protein 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=1LA1 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Ashcroft, A.E.]]
+[[Category: Ashcroft, A E.]]
 [[Category: Brinker, A.]]
-[[Category: Coyle, J.E.]]
+[[Category: Coyle, J E.]]
-[[Category: Hartl, U.F.]]
+[[Category: Hartl, U F.]]
 [[Category: Hayer-Hartl, M.]]
 [[Category: Jager, J.]]
 [[Category: Kaiser, M.]]
 [[Category: Moroder, L.]]
-[[Category: Parsons, M.R.]]
+[[Category: Parsons, M R.]]
-[[Category: Radford, S.E.]]
+[[Category: Radford, S E.]]
 [[Category: Weber, F.]]
 [[Category: molecular chaperone]]
 [[Category: protein folding]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:25:06 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:58 2008''