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| | ==Structure of the hypothetical Arabidopsis thaliana protein At1g16640.1== | | ==Structure of the hypothetical Arabidopsis thaliana protein At1g16640.1== |
| - | <StructureSection load='1yel' size='340' side='right'caption='[[1yel]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1yel' size='340' side='right'caption='[[1yel]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1yel]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YEL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YEL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1yel]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YEL FirstGlance]. <br> |
| - | </td></tr><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=1yel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yel OCA], [http://pdbe.org/1yel PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yel RCSB], [http://www.ebi.ac.uk/pdbsum/1yel PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yel ProSAT], [http://www.topsan.org/Proteins/CESG/1yel TOPSAN]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yel OCA], [https://pdbe.org/1yel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yel RCSB], [https://www.ebi.ac.uk/pdbsum/1yel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yel ProSAT], [https://www.topsan.org/Proteins/CESG/1yel TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Y1664_ARATH Y1664_ARATH] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Lytle BL]] |
| - | [[Category: Lytle, B L]] | + | [[Category: Peterson FC]] |
| - | [[Category: Peterson, F C]] | + | [[Category: Volkman BF]] |
| - | [[Category: Volkman, B F]] | + | [[Category: Waltner JK]] |
| - | [[Category: Waltner, J K]] | + | |
| - | [[Category: Cesg]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
Y1664_ARATH
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A novel DNA binding motif, the B3 domain, has been identified in a number of transcription factors specific to higher plant species, and was recently found to define a new protein fold. Here we report the second structure of a B3 domain, that of the Arabidopsis thaliana protein, At1g16640. As part of an effort to 'rescue' structural genomics targets deemed unsuitable for structure determination as full-length proteins, we applied a combined bioinformatic and experimental strategy to identify an optimal construct containing a predicted conserved domain. By screening a series of N- and C-terminally truncated At1g16640 fragments, we isolated a stable folded domain that met our criteria for structural analysis by NMR spectroscopy. The structure of the B3 domain of At1g16640 consists of a seven-stranded beta-sheet arranged in an open barrel and two short alpha-helices, one at each end of the barrel. While At1g16640 is quite distinct from previously characterized B3 domain proteins in terms of amino acid sequence similarity, it adopts the same novel fold that was recently revealed by the RAV1 B3 domain structure. However, putative DNA-binding elements conserved in B3 domains from the RAV, ARF, and ABI3/VP1 subfamilies are largely absent in At1g16640, perhaps suggesting that B3 domains could function in contexts other than transcriptional regulation.
Structure of the B3 domain from Arabidopsis thaliana protein At1g16640.,Waltner JK, Peterson FC, Lytle BL, Volkman BF Protein Sci. 2005 Sep;14(9):2478-83. Epub 2005 Aug 4. PMID:16081658[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Waltner JK, Peterson FC, Lytle BL, Volkman BF. Structure of the B3 domain from Arabidopsis thaliana protein At1g16640. Protein Sci. 2005 Sep;14(9):2478-83. Epub 2005 Aug 4. PMID:16081658 doi:10.1110/ps.051606305
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