1zfd: Difference between revisions
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==SWI5 ZINC FINGER DOMAIN 2, NMR, 45 STRUCTURES== | ==SWI5 ZINC FINGER DOMAIN 2, NMR, 45 STRUCTURES== | ||
<StructureSection load='1zfd' size='340' side='right'caption='[[1zfd | <StructureSection load='1zfd' size='340' side='right'caption='[[1zfd]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1zfd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1zfd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZFD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZFD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1zfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zfd OCA], [https://pdbe.org/1zfd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zfd RCSB], [https://www.ebi.ac.uk/pdbsum/1zfd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zfd 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=1zfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zfd OCA], [https://pdbe.org/1zfd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zfd RCSB], [https://www.ebi.ac.uk/pdbsum/1zfd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zfd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SWI5_YEAST SWI5_YEAST] Determines the mother-cell-specific transcription of the HO endonuclease gene that is responsible for the initiation of mating-type switching in yeast. Recognizes a specific sequence in the promoter of the HO gene. Activates EGT2 transcription in a concentration-dependent manner. Synthesized during G2 and early mitosis. | |||
== 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: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Klug | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Nakaseko | [[Category: Klug A]] | ||
[[Category: Neuhaus | [[Category: Nakaseko Y]] | ||
[[Category: Rhodes | [[Category: Neuhaus D]] | ||
[[Category: Schwabe | [[Category: Rhodes D]] | ||
[[Category: Schwabe JWR]] | |||
Latest revision as of 11:10, 15 May 2024
SWI5 ZINC FINGER DOMAIN 2, NMR, 45 STRUCTURESSWI5 ZINC FINGER DOMAIN 2, NMR, 45 STRUCTURES
Structural highlights
FunctionSWI5_YEAST Determines the mother-cell-specific transcription of the HO endonuclease gene that is responsible for the initiation of mating-type switching in yeast. Recognizes a specific sequence in the promoter of the HO gene. Activates EGT2 transcription in a concentration-dependent manner. Synthesized during G2 and early mitosis. 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 PubMedThis paper describes the detailed three-dimensional structures of two zinc-finger domains from the yeast transcription factor SWI5, calculated using the results of the n.m.r. experiments described in the accompanying paper. The structure of finger 2 is essentially similar to those previously obtained by others for isolated, synthetic single zinc-finger domains in solution, and for the three zinc-finger peptide Zif268 in its crystalline complex with DNA. The N-terminal half of the sequence forms a two-stranded, irregular beta-sheet containing both of the metal-binding cysteine residues, while the remainder of the structure forms a helix. Approximately the first half of this helix is alpha-helical, whereas the C-terminal portion, including the two metal-binding histidine residues, is 3(10) helical. Four invariant hydrophobic residues form a core to the structure. In contrast to all previously described structures of zinc-finger domains, finger 1 has an additional strand in the beta-sheet, formed by residues N-terminal to the formal start of the finger motif. This additional strand plays a role in stabilising the folded form of finger 1, since a two-finger peptide lacking the N-terminal residues showed folded structure in finger 2 but not in finger 1. Solution structures of two zinc-finger domains from SWI5 obtained using two-dimensional 1H nuclear magnetic resonance spectroscopy. A zinc-finger structure with a third strand of beta-sheet.,Neuhaus D, Nakaseko Y, Schwabe JW, Klug A J Mol Biol. 1992 Nov 20;228(2):637-51. PMID:1453468[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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