1mft
From Proteopedia
(New page: 200px<br /><applet load="1mft" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mft, resolution 2.50Å" /> '''Crystal Structure Of...) |
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| - | [[Image:1mft.gif|left|200px]]<br /><applet load="1mft" size=" | + | [[Image:1mft.gif|left|200px]]<br /><applet load="1mft" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mft, resolution 2.50Å" /> | caption="1mft, resolution 2.50Å" /> | ||
'''Crystal Structure Of Four-Helix Bundle Model'''<br /> | '''Crystal Structure Of Four-Helix Bundle Model'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Although the analysis and design of turns that connect the strands in | + | Although the analysis and design of turns that connect the strands in antiparallel beta-hairpins has reached an advanced state, much less is known concerning turns between antiparallel helices in helical hairpins. We have conducted an analysis of the structures and sequence preferences of two types of interhelical turns, each of which connects the two helices by a two-residue linker in an alphaL-beta conformation. Based on this analysis, it became apparent that the turn introduced into a designed four-helix bundle protein, DF1, did not occur within an optimal structural context. DF1 is a dimeric model for the diiron class of proteins. A longer loop with a beta-alphaR-beta conformation was inserted between two helices in the protein, and a sequence was chosen to stabilize its conformation. X-ray crystallography and NMR analysis of the protein showed the structure to be in excellent agreement with design. |
==About this Structure== | ==About this Structure== | ||
| - | 1MFT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MFT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MFT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Geremia, S.]] | [[Category: Geremia, S.]] | ||
[[Category: Kaplan, J.]] | [[Category: Kaplan, J.]] | ||
| - | [[Category: Lahr, S | + | [[Category: Lahr, S J.]] |
[[Category: North, B.]] | [[Category: North, B.]] | ||
| - | [[Category: Stayrook, S | + | [[Category: Stayrook, S E.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: alpha-helical bundle]] | [[Category: alpha-helical bundle]] | ||
| Line 24: | Line 24: | ||
[[Category: protein design]] | [[Category: protein design]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:49 2008'' |
Revision as of 11:54, 21 February 2008
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Crystal Structure Of Four-Helix Bundle Model
Overview
Although the analysis and design of turns that connect the strands in antiparallel beta-hairpins has reached an advanced state, much less is known concerning turns between antiparallel helices in helical hairpins. We have conducted an analysis of the structures and sequence preferences of two types of interhelical turns, each of which connects the two helices by a two-residue linker in an alphaL-beta conformation. Based on this analysis, it became apparent that the turn introduced into a designed four-helix bundle protein, DF1, did not occur within an optimal structural context. DF1 is a dimeric model for the diiron class of proteins. A longer loop with a beta-alphaR-beta conformation was inserted between two helices in the protein, and a sequence was chosen to stabilize its conformation. X-ray crystallography and NMR analysis of the protein showed the structure to be in excellent agreement with design.
About this Structure
1MFT is a Protein complex structure of sequences from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Analysis and design of turns in alpha-helical hairpins., Lahr SJ, Engel DE, Stayrook SE, Maglio O, North B, Geremia S, Lombardi A, DeGrado WF, J Mol Biol. 2005 Mar 11;346(5):1441-54. Epub 2005 Jan 13. PMID:15713492
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