1ncs: Difference between revisions
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==NMR STUDY OF SWI5 ZINC FINGER DOMAIN 1== | |||
<StructureSection load='1ncs' size='340' side='right'caption='[[1ncs]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ncs]] 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=1NCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NCS FirstGlance]. <br> | |||
</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=1ncs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ncs OCA], [https://pdbe.org/1ncs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ncs RCSB], [https://www.ebi.ac.uk/pdbsum/1ncs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ncs ProSAT]</span></td></tr> | |||
</table> | |||
== 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 == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nc/1ncs_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ncs ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
BACKGROUND: The 2Cys-2His (C2-H2) zinc finger is a protein domain commonly used for sequence-specific DNA recognition. The zinc fingers of the yeast transcription factors SWI5 and ACE2 share strong sequence homology, which extends into a region N-terminal to the first finger, suggesting that the DNA-binding domains of these two proteins include additional structural elements. RESULTS: Structural analysis of the zinc fingers of SWI5 reveals that a 15 residue region N-terminal to the finger motifs forms part of the structure of the first finger domain, adding a beta strand and a helix not previously observed in other zinc finger structures. Sequence analysis suggests that other zinc finger proteins may also have this structure. Biochemical studies show that this additional structure increases DNA-binding affinity. CONCLUSIONS: The structural analysis presented reveals a novel zinc finger structure in which additional structural elements have been added to the C2-H2 zinc finger fold. This additional structure may enhance stability and has implications for DNA recognition by extending the potential DNA-binding surface of a single zinc finger domain. | |||
The solution structure of the first zinc finger domain of SWI5: a novel structural extension to a common fold.,Dutnall RN, Neuhaus D, Rhodes D Structure. 1996 May 15;4(5):599-611. PMID:8736557<ref>PMID:8736557</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ncs" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Dutnall | [[Category: Dutnall RN]] | ||
[[Category: Neuhaus | [[Category: Neuhaus D]] | ||
[[Category: Rhodes | [[Category: Rhodes D]] | ||
Latest revision as of 11:53, 22 May 2024
NMR STUDY OF SWI5 ZINC FINGER DOMAIN 1NMR STUDY OF SWI5 ZINC FINGER DOMAIN 1
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 PubMedBACKGROUND: The 2Cys-2His (C2-H2) zinc finger is a protein domain commonly used for sequence-specific DNA recognition. The zinc fingers of the yeast transcription factors SWI5 and ACE2 share strong sequence homology, which extends into a region N-terminal to the first finger, suggesting that the DNA-binding domains of these two proteins include additional structural elements. RESULTS: Structural analysis of the zinc fingers of SWI5 reveals that a 15 residue region N-terminal to the finger motifs forms part of the structure of the first finger domain, adding a beta strand and a helix not previously observed in other zinc finger structures. Sequence analysis suggests that other zinc finger proteins may also have this structure. Biochemical studies show that this additional structure increases DNA-binding affinity. CONCLUSIONS: The structural analysis presented reveals a novel zinc finger structure in which additional structural elements have been added to the C2-H2 zinc finger fold. This additional structure may enhance stability and has implications for DNA recognition by extending the potential DNA-binding surface of a single zinc finger domain. The solution structure of the first zinc finger domain of SWI5: a novel structural extension to a common fold.,Dutnall RN, Neuhaus D, Rhodes D Structure. 1996 May 15;4(5):599-611. PMID:8736557[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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