1nay
From Proteopedia
(New page: 200px<br /><applet load="1nay" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nay, resolution 2.60Å" /> '''GPP-Foldon:X-ray str...) |
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| - | [[Image:1nay.gif|left|200px]]<br /><applet load="1nay" size=" | + | [[Image:1nay.gif|left|200px]]<br /><applet load="1nay" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nay, resolution 2.60Å" /> | caption="1nay, resolution 2.60Å" /> | ||
'''GPP-Foldon:X-ray structure'''<br /> | '''GPP-Foldon:X-ray structure'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In a designed fusion protein the trimeric domain foldon from bacteriophage | + | In a designed fusion protein the trimeric domain foldon from bacteriophage T4 fibritin was connected to the C terminus of the collagen model peptide (GlyProPro)(10) by a short Gly-Ser linker to facilitate formation of the three-stranded collagen triple helix. Crystal structure analysis at 2.6 A resolution revealed conformational changes within the interface of both domains compared with the structure of the isolated molecules. A striking feature is an angle of 62.5 degrees between the symmetry axis of the foldon trimer and the axis of the triple helix. The melting temperature of (GlyProPro)(10) in the designed fusion protein (GlyProPro)(10)foldon is higher than that of isolated (GlyProPro)(10,) which suggests an entropic stabilization compensating for the destabilization at the interface. |
==About this Structure== | ==About this Structure== | ||
| - | 1NAY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1NAY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NAY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: collagen assembly]] | [[Category: collagen assembly]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:11 2008'' |
Revision as of 12:04, 21 February 2008
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GPP-Foldon:X-ray structure
Overview
In a designed fusion protein the trimeric domain foldon from bacteriophage T4 fibritin was connected to the C terminus of the collagen model peptide (GlyProPro)(10) by a short Gly-Ser linker to facilitate formation of the three-stranded collagen triple helix. Crystal structure analysis at 2.6 A resolution revealed conformational changes within the interface of both domains compared with the structure of the isolated molecules. A striking feature is an angle of 62.5 degrees between the symmetry axis of the foldon trimer and the axis of the triple helix. The melting temperature of (GlyProPro)(10) in the designed fusion protein (GlyProPro)(10)foldon is higher than that of isolated (GlyProPro)(10,) which suggests an entropic stabilization compensating for the destabilization at the interface.
About this Structure
1NAY is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Collagen stabilization at atomic level: crystal structure of designed (GlyProPro)10foldon., Stetefeld J, Frank S, Jenny M, Schulthess T, Kammerer RA, Boudko S, Landwehr R, Okuyama K, Engel J, Structure. 2003 Mar;11(3):339-46. PMID:12623021
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