1zfd: Difference between revisions

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{{Seed}}
[[Image:1zfd.png|left|200px]]


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==SWI5 ZINC FINGER DOMAIN 2, NMR, 45 STRUCTURES==
The line below this paragraph, containing "STRUCTURE_1zfd", creates the "Structure Box" on the page.
<StructureSection load='1zfd' size='340' side='right'caption='[[1zfd]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
{{STRUCTURE_1zfd|  PDB=1zfd  |  SCENE=  }}
<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>
== 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/zf/1zfd_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=1zfd ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
This 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.


===SWI5 ZINC FINGER DOMAIN 2, NMR, 45 STRUCTURES===
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<ref>PMID:1453468</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_1453468}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1zfd" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 1453468 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_1453468}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1ZFD is a 1 chain structure of sequence from [http://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].
 
==Reference==
<ref group="xtra">PMID:1453468</ref><references group="xtra"/>
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Klug, A.]]
[[Category: Klug A]]
[[Category: Nakaseko, Y.]]
[[Category: Nakaseko Y]]
[[Category: Neuhaus, D.]]
[[Category: Neuhaus D]]
[[Category: Rhodes, D.]]
[[Category: Rhodes D]]
[[Category: Schwabe, J W.R.]]
[[Category: Schwabe JWR]]
[[Category: Dna binding motif]]
[[Category: Zinc finger dna binding domain]]
 
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Retrieved from "https://proteopedia.org/1zfd"