2l1o

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(Difference between revisions)

Revision as of 09:30, 11 September 2015

Zinc to cadmium replacement in the A. thaliana SUPERMAN Cys2His2 zinc finger induces structural rearrangements of typical DNA base determinant positions

Structural highlights

2l1o is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[SUP_ARATH] Probable transcriptional regulator considered as cadastral protein that acts indirectly to prevent the B class homeotic proteins APETALA3 and perhaps PISTILLATA from acting in the gynoecial whorl. Principal function is to balance cell proliferation in the third and fourth whorls of developing flowers thereby maintaining the boundary between stamens and carpels. May fulfill this role by repressing genes implicated in cell division. Plays equally a role in the determinacy of the floral meristem. Is also required for normal ovule development.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Among heavy metals, whose toxicity cause a steadily increasing of environmental pollution, cadmium is of special concern due to its relatively high mobility in soils and potential toxicity at low concentrations. Given their ubiquitous role, zinc fingers domains have been proposed as mediators for the toxic and carcinogenic effects exerted by xenobiotic metals. To verify the structural effects of zinc replacement by cadmium in zinc fingers we have determined the high resolution structure of the single Cys(2) His(2) zinc finger of the A. thaliana Superman protein (SUP37) complexed to the cadmium ion by means of UV-Vis and NMR techniques. SUP37 is able to bind Cd(II) though with a dissociation constant higher than that measured for Zn(II). Cd-SUP37 retains the betabetaalpha fold but experiences a global structural rearrangement affecting both the relative orientation of the secondary structure elements and the position of side chains involved in DNA recognition: among them Ser17 side chain, which we show to be essential for DNA binding, experiences the largest displacement. (c) 2011 Wiley Periodicals, Inc. Biopolymers, 2011.

Zinc to cadmium replacement in the A. thaliana SUPERMAN Cys(2) His(2) zinc finger induces structural rearrangements of typical DNA base determinant positions.,Malgieri G, Zaccaro L, Leone M, Bucci E, Esposito S, Baglivo I, Del Gatto A, Russo L, Scandurra R, Pedone PV, Fattorusso R, Isernia C Biopolymers. 2011 May 25. doi: 10.1002/bip.21680. PMID:21618209^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sakai H, Medrano LJ, Meyerowitz EM. Role of SUPERMAN in maintaining Arabidopsis floral whorl boundaries. Nature. 1995 Nov 9;378(6553):199-203. PMID:7477325 doi:http://dx.doi.org/10.1038/378199a0
↑ Schultz EA, Pickett FB, Haughn GW. The FLO10 Gene Product Regulates the Expression Domain of Homeotic Genes AP3 and PI in Arabidopsis Flowers. Plant Cell. 1991 Nov;3(11):1221-1237. PMID:12324589 doi:http://dx.doi.org/10.1105/tpc.3.11.1221
↑ Bowman JL, Sakai H, Jack T, Weigel D, Mayer U, Meyerowitz EM. SUPERMAN, a regulator of floral homeotic genes in Arabidopsis. Development. 1992 Mar;114(3):599-615. PMID:1352237
↑ Sakai H, Krizek BA, Jacobsen SE, Meyerowitz EM. Regulation of SUP expression identifies multiple regulators involved in arabidopsis floral meristem development. Plant Cell. 2000 Sep;12(9):1607-18. PMID:11006335
↑ Hiratsu K, Ohta M, Matsui K, Ohme-Takagi M. The SUPERMAN protein is an active repressor whose carboxy-terminal repression domain is required for the development of normal flowers. FEBS Lett. 2002 Mar 13;514(2-3):351-4. PMID:11943180
↑ Malgieri G, Zaccaro L, Leone M, Bucci E, Esposito S, Baglivo I, Del Gatto A, Russo L, Scandurra R, Pedone PV, Fattorusso R, Isernia C. Zinc to cadmium replacement in the A. thaliana SUPERMAN Cys(2) His(2) zinc finger induces structural rearrangements of typical DNA base determinant positions. Biopolymers. 2011 May 25. doi: 10.1002/bip.21680. PMID:21618209 doi:10.1002/bip.21680

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2l1o"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=2l1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l1o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l1o RCSB], [http://www.ebi.ac.uk/pdbsum/2l1o PDBsum]</span></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=2l1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l1o OCA], [http://pdbe.org/2l1o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l1o RCSB], [http://www.ebi.ac.uk/pdbsum/2l1o PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2l1o" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2l1o

From Proteopedia

Revision as of 09:30, 11 September 2015

Zinc to cadmium replacement in the A. thaliana SUPERMAN Cys2His2 zinc finger induces structural rearrangements of typical DNA base determinant positions

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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