1wy3
From Proteopedia
(New page: 200px<br /><applet load="1wy3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wy3, resolution 0.95Å" /> '''Chicken villin subdo...) |
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| - | [[Image:1wy3.gif|left|200px]]<br /><applet load="1wy3" size=" | + | [[Image:1wy3.gif|left|200px]]<br /><applet load="1wy3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wy3, resolution 0.95Å" /> | caption="1wy3, resolution 0.95Å" /> | ||
'''Chicken villin subdomain HP-35, K65(NLE), N68H, pH7.0'''<br /> | '''Chicken villin subdomain HP-35, K65(NLE), N68H, pH7.0'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 35-residue subdomain of the villin headpiece (HP35) is a small | + | The 35-residue subdomain of the villin headpiece (HP35) is a small ultrafast folding protein that is being intensely studied by experiments, theory, and simulations. We have solved the x-ray structures of HP35 and its fastest folding mutant [K24 norleucine (nL)] to atomic resolution and compared their experimentally measured folding kinetics by using laser temperature jump. The structures, which are in different space groups, are almost identical to each other but differ significantly from previously solved NMR structures. Hence, the differences between the x-ray and NMR structures are probably not caused by lattice contacts or crystal/solution differences, but reflect the higher accuracy of the x-ray structures. The x-ray structures reveal important details of packing of the hydrophobic core and some additional features, such as cross-helical H bonds. Comparison of the x-ray structures indicates that the nL substitution produces only local perturbations. Consequently, the finding that the small stabilization by the mutation is completely reflected in an increased folding rate suggests that this region of the protein is as structured in the transition state as in the folded structure. It is therefore a target for engineering to increase the folding rate of the subdomain from approximately 0.5 micros(-1) for the nL mutant to the estimated theoretical speed limit of approximately 3 micros(-1). |
==About this Structure== | ==About this Structure== | ||
| - | 1WY3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1WY3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WY3 OCA]. |
==Reference== | ==Reference== | ||
High-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein., Chiu TK, Kubelka J, Herbst-Irmer R, Eaton WA, Hofrichter J, Davies DR, Proc Natl Acad Sci U S A. 2005 May 24;102(21):7517-22. Epub 2005 May 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15894611 15894611] | High-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein., Chiu TK, Kubelka J, Herbst-Irmer R, Eaton WA, Hofrichter J, Davies DR, Proc Natl Acad Sci U S A. 2005 May 24;102(21):7517-22. Epub 2005 May 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15894611 15894611] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chiu, T | + | [[Category: Chiu, T K.]] |
| - | [[Category: Davies, D | + | [[Category: Davies, D R.]] |
| - | [[Category: Eaton, W | + | [[Category: Eaton, W A.]] |
[[Category: Herbst-Irmer, R.]] | [[Category: Herbst-Irmer, R.]] | ||
[[Category: Hofrichter, J.]] | [[Category: Hofrichter, J.]] | ||
| Line 20: | Line 20: | ||
[[Category: villin headgroup subdomain]] | [[Category: villin headgroup subdomain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:49:14 2008'' |
Revision as of 13:49, 21 February 2008
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Chicken villin subdomain HP-35, K65(NLE), N68H, pH7.0
Overview
The 35-residue subdomain of the villin headpiece (HP35) is a small ultrafast folding protein that is being intensely studied by experiments, theory, and simulations. We have solved the x-ray structures of HP35 and its fastest folding mutant [K24 norleucine (nL)] to atomic resolution and compared their experimentally measured folding kinetics by using laser temperature jump. The structures, which are in different space groups, are almost identical to each other but differ significantly from previously solved NMR structures. Hence, the differences between the x-ray and NMR structures are probably not caused by lattice contacts or crystal/solution differences, but reflect the higher accuracy of the x-ray structures. The x-ray structures reveal important details of packing of the hydrophobic core and some additional features, such as cross-helical H bonds. Comparison of the x-ray structures indicates that the nL substitution produces only local perturbations. Consequently, the finding that the small stabilization by the mutation is completely reflected in an increased folding rate suggests that this region of the protein is as structured in the transition state as in the folded structure. It is therefore a target for engineering to increase the folding rate of the subdomain from approximately 0.5 micros(-1) for the nL mutant to the estimated theoretical speed limit of approximately 3 micros(-1).
About this Structure
1WY3 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
High-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein., Chiu TK, Kubelka J, Herbst-Irmer R, Eaton WA, Hofrichter J, Davies DR, Proc Natl Acad Sci U S A. 2005 May 24;102(21):7517-22. Epub 2005 May 13. PMID:15894611
Page seeded by OCA on Thu Feb 21 15:49:14 2008
