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| - | [[Image:2bh8.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2bh8.png|left|200px]] |
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| | {{STRUCTURE_2bh8| PDB=2bh8 | SCENE= }} | | {{STRUCTURE_2bh8| PDB=2bh8 | SCENE= }} |
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| - | '''COMBINATORIAL PROTEIN 1B11'''
| + | ===COMBINATORIAL PROTEIN 1B11=== |
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| - | ==Overview==
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| - | It has been suggested that protein domains evolved by the non-homologous recombination of building blocks of subdomain size. In earlier work we attempted to recapitulate domain evolution in vitro. We took a polypeptide segment comprising three beta-strands in the monomeric, five-stranded beta-barrel cold shock protein (CspA) of Escherichia coli as a building block. This segment corresponds to a complete exon in homologous eukaryotic proteins and includes residues that nucleate folding in CspA. We recombined this segment at random with fragments of natural proteins and succeeded in generating a range of folded chimaeric proteins. We now present the crystal structure of one such combinatorial protein, 1b11, a 103-residue polypeptide that includes segments from CspA and the S1 domain of the 30S ribosomal subunit of E. coli. The structure reveals a segment-swapped, six-stranded beta-barrel of unique architecture that assembles to a tetramer. Surprisingly, the CspA segment retains its structural identity in 1b11, recapitulating its original fold and deforming the structure of the S1 segment as necessary to complete a barrel. Our work provides structural evidence that (i) random shuffling of nonhomologous polypeptide segments can lead to folded proteins and unique architectures, (ii) many structural features of the segments are retained, and (iii) some segments can act as templates around which the rest of the protein folds.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15671167}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15671167 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15671167}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Transcription regulation]] | | [[Category: Transcription regulation]] |
| | [[Category: Unique architecture]] | | [[Category: Unique architecture]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:17:00 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:08:53 2008'' |
Revision as of 14:08, 27 July 2008
Template:STRUCTURE 2bh8
COMBINATORIAL PROTEIN 1B11
Template:ABSTRACT PUBMED 15671167
About this Structure
2BH8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
A segment of cold shock protein directs the folding of a combinatorial protein., de Bono S, Riechmann L, Girard E, Williams RL, Winter G, Proc Natl Acad Sci U S A. 2005 Feb 1;102(5):1396-401. Epub 2005 Jan 25. PMID:15671167
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