1mft
From Proteopedia
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| - | [[Image:1mft.gif|left|200px]] | + | [[Image:1mft.gif|left|200px]] |
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| - | '''Crystal Structure Of Four-Helix Bundle Model''' | + | {{Structure |
| + | |PDB= 1mft |SIZE=350|CAPTION= <scene name='initialview01'>1mft</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure Of Four-Helix Bundle Model''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MFT is a [ | + | 1MFT is a [[Protein complex]] structure of sequences 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=1MFT OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15713492 15713492] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: protein design]] | [[Category: protein design]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:43:00 2008'' |
Revision as of 10:43, 20 March 2008
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| , resolution 2.50Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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