1sn9
From Proteopedia
(New page: 200px<br /><applet load="1sn9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sn9, resolution 1.20Å" /> '''An Oligomeric Domain...) |
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| - | [[Image:1sn9.gif|left|200px]]<br /><applet load="1sn9" size=" | + | [[Image:1sn9.gif|left|200px]]<br /><applet load="1sn9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sn9, resolution 1.20Å" /> | caption="1sn9, resolution 1.20Å" /> | ||
'''An Oligomeric Domain-Swapped Beta-Beta-Alpha Mini-Protein'''<br /> | '''An Oligomeric Domain-Swapped Beta-Beta-Alpha Mini-Protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The x-ray crystal structure of an oligomeric miniprotein has been | + | The x-ray crystal structure of an oligomeric miniprotein has been determined to a 1.2-A resolution by means of multiwavelength anomalous diffraction phasing with selenomethionine analogs that retain the biophysical characteristics of the native peptide. Peptide 1, comprising alpha and beta secondary structure elements with only 21 aa per monomer, associates as a discrete tetramer. The peptide adopts a previously uncharacterized quaternary structure in which alpha and beta components interact to form a tightly packed and well defined hydrophobic core. The structure provides insight into the origins of the unusual thermal stability of the oligomer. The miniprotein shares many characteristics of larger proteins, including cooperative folding, lack of 1-anilino-8-naphthalene sulfonate binding, and limited deuterium exchange, and possesses a buried surface area typical of native proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1SN9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1SN9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SN9 OCA]. |
==Reference== | ==Reference== | ||
X-ray structure analysis of a designed oligomeric miniprotein reveals a discrete quaternary architecture., Ali MH, Peisach E, Allen KN, Imperiali B, Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12183-8. Epub 2004 Aug 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15302930 15302930] | X-ray structure analysis of a designed oligomeric miniprotein reveals a discrete quaternary architecture., Ali MH, Peisach E, Allen KN, Imperiali B, Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12183-8. Epub 2004 Aug 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15302930 15302930] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Ali, M | + | [[Category: Ali, M H.]] |
| - | [[Category: Allen, K | + | [[Category: Allen, K N.]] |
[[Category: Imperiali, B.]] | [[Category: Imperiali, B.]] | ||
[[Category: Peisach, E.]] | [[Category: Peisach, E.]] | ||
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[[Category: protein design]] | [[Category: protein design]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:03:16 2008'' |
Revision as of 13:03, 21 February 2008
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An Oligomeric Domain-Swapped Beta-Beta-Alpha Mini-Protein
Overview
The x-ray crystal structure of an oligomeric miniprotein has been determined to a 1.2-A resolution by means of multiwavelength anomalous diffraction phasing with selenomethionine analogs that retain the biophysical characteristics of the native peptide. Peptide 1, comprising alpha and beta secondary structure elements with only 21 aa per monomer, associates as a discrete tetramer. The peptide adopts a previously uncharacterized quaternary structure in which alpha and beta components interact to form a tightly packed and well defined hydrophobic core. The structure provides insight into the origins of the unusual thermal stability of the oligomer. The miniprotein shares many characteristics of larger proteins, including cooperative folding, lack of 1-anilino-8-naphthalene sulfonate binding, and limited deuterium exchange, and possesses a buried surface area typical of native proteins.
About this Structure
1SN9 is a Protein complex structure of sequences from [1] with and as ligands. Full crystallographic information is available from OCA.
Reference
X-ray structure analysis of a designed oligomeric miniprotein reveals a discrete quaternary architecture., Ali MH, Peisach E, Allen KN, Imperiali B, Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12183-8. Epub 2004 Aug 9. PMID:15302930
Page seeded by OCA on Thu Feb 21 15:03:16 2008
