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| | <StructureSection load='3bd1' size='340' side='right'caption='[[3bd1]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='3bd1' size='340' side='right'caption='[[3bd1]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3bd1]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Xylella_fastidiosa_ann-1 Xylella fastidiosa ann-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BD1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3BD1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3bd1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Xylella_fastidiosa_subsp._sandyi_Ann-1 Xylella fastidiosa subsp. sandyi Ann-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BD1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pij|2pij]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3bd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bd1 OCA], [http://pdbe.org/3bd1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bd1 RCSB], [http://www.ebi.ac.uk/pdbsum/3bd1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bd1 ProSAT]</span></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=3bd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bd1 OCA], [https://pdbe.org/3bd1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bd1 RCSB], [https://www.ebi.ac.uk/pdbsum/3bd1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bd1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Xylella fastidiosa ann-1]] | + | [[Category: Xylella fastidiosa subsp. sandyi Ann-1]] |
| - | [[Category: Cordes, M H]] | + | [[Category: Cordes MH]] |
| - | [[Category: Hall, B M]] | + | [[Category: Hall BM]] |
| - | [[Category: Montfort, W R]] | + | [[Category: Montfort WR]] |
| - | [[Category: Roberts, S A]] | + | [[Category: Roberts SA]] |
| - | [[Category: Helix-turn-helix]]
| + | |
| - | [[Category: Prophage]]
| + | |
| - | [[Category: Structural evolution]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription factor]]
| + | |
| Structural highlights
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
Proteins that share common ancestry may differ in structure and function because of divergent evolution of their amino acid sequences. For a typical diverse protein superfamily, the properties of a few scattered members are known from experiment. A satisfying picture of functional and structural evolution in relation to sequence changes, however, may require characterization of a larger, well chosen subset. Here, we employ a "stepping-stone" method, based on transitive homology, to target sequences intermediate between two related proteins with known divergent properties. We apply the approach to the question of how new protein folds can evolve from preexisting folds and, in particular, to an evolutionary change in secondary structure and oligomeric state in the Cro family of bacteriophage transcription factors, initially identified by sequence-structure comparison of distant homologs from phages P22 and lambda. We report crystal structures of two Cro proteins, Xfaso 1 and Pfl 6, with sequences intermediate between those of P22 and lambda. The domains show 40% sequence identity but differ by switching of alpha-helix to beta-sheet in a C-terminal region spanning approximately 25 residues. Sedimentation analysis also suggests a correlation between helix-to-sheet conversion and strengthened dimerization.
Transitive homology-guided structural studies lead to discovery of Cro proteins with 40% sequence identity but different folds.,Roessler CG, Hall BM, Anderson WJ, Ingram WM, Roberts SA, Montfort WR, Cordes MH Proc Natl Acad Sci U S A. 2008 Feb 19;105(7):2343-8. Epub 2008 Jan 28. PMID:18227506[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Roessler CG, Hall BM, Anderson WJ, Ingram WM, Roberts SA, Montfort WR, Cordes MH. Transitive homology-guided structural studies lead to discovery of Cro proteins with 40% sequence identity but different folds. Proc Natl Acad Sci U S A. 2008 Feb 19;105(7):2343-8. Epub 2008 Jan 28. PMID:18227506
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