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4o60

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'''Unreleased structure'''
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==Structure of ankyrin repeat protein==
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<StructureSection load='4o60' size='340' side='right' caption='[[4o60]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4o60]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O60 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qfv|4qfv]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o60 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o60 RCSB], [http://www.ebi.ac.uk/pdbsum/4o60 PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A highly diverse DNA library coding for ankyrin seven-repeat proteins (ANK-N5C) was designed and constructed by a PCR-based combinatorial assembly strategy. A bacterial melibiose fermentation assay was adapted for in vivo functional screen. We isolated a transcription blocker that completely inhibits the melibiose-dependent expression of alpha-galactosidase (MelA) and melibiose permease (MelB) of Escherichia coli by specifically preventing activation of the melAB operon. High-resolution crystal structural determination reveals that the designed ANK-N5C protein has a typical ankyrin fold, and the specific transcription blocker, ANK-N5C-281, forms a domain-swapped dimer. Functional tests suggest that the activity of MelR, a DNA-binding transcription activator and a member of AraC family of transcription factors, is inhibited by ANK-N5C-281 protein. All ANK-N5C proteins are expected to have a concave binding area with negative surface potential, suggesting that the designed ANK-N5C library proteins may facilitate the discovery of binders recognizing structural motifs with positive surface potential, like in DNA-binding proteins. Overall, our results show that the established library is a useful tool for the discovery of novel bioactive reagents.
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The entry 4o60 is ON HOLD until Mar 25 2016
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A transcription blocker isolated from a designed repeat protein combinatorial library by in vivo functional screen.,Tikhonova EB, Ethayathulla AS, Su Y, Hariharan P, Xie S, Guan L Sci Rep. 2015 Jan 28;5:8070. doi: 10.1038/srep08070. PMID:25627011<ref>PMID:25627011</ref>
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Authors: Ethayathulla, A.S., Lan, G.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Structure of ankyrin repeat protein
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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[[Category: Ethayathulla, A.S]]
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__TOC__
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</StructureSection>
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[[Category: Ethayathulla, A S]]
[[Category: Lan, G]]
[[Category: Lan, G]]
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[[Category: Ankyrin]]
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[[Category: De novo protein]]
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[[Category: Designed ankyrin repeat]]

Revision as of 13:58, 26 March 2015

Structure of ankyrin repeat protein

4o60, resolution 2.52Å

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