1un6

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(Difference between revisions)

Current revision

THE CRYSTAL STRUCTURE OF A ZINC FINGER - RNA COMPLEX REVEALS TWO MODES OF MOLECULAR RECOGNITION

Structural highlights

1un6 is a 5 chain structure with sequence from Xenopus laevis. The March 2007 RCSB PDB Molecule of the Month feature on Zinc Fingers by David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.1Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TF3A_XENLA Acts as both a positive transcription factor for 5S RNA genes and a specific RNA binding protein that complexes with 5S RNA in oocytes to form the 7S ribonucleoprotein storage particle. May play an essential role in the developmental change in 5S RNA gene expression. Interacts with the internal control region (ICR) of approximately 50 bases within the 5S RNA genes, is required for correct transcription of these genes by RNA polymerase III. Also binds the transcribed 5S RNA's.

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

Zinc-finger proteins of the classical Cys2His2 type are the most frequently used class of transcription factor and account for about 3% of genes in the human genome. The zinc-finger motif was discovered during biochemical studies on the transcription factor TFIIIA, which regulates the 5S ribosomal RNA genes of Xenopus laevis. Zinc-fingers mostly interact with DNA, but TFIIIA binds not only specifically to the promoter DNA, but also to 5S RNA itself. Increasing evidence indicates that zinc-fingers are more widely used to recognize RNA. There have been numerous structural studies on DNA binding, but none on RNA binding by zinc-finger proteins. Here we report the crystal structure of a three-finger complex with 61 bases of RNA, derived from the central regions of the complete nine-finger TFIIIA-5S RNA complex. The structure reveals two modes of zinc-finger binding, both of which differ from that in common use for DNA: first, the zinc-fingers interact with the backbone of a double helix; and second, the zinc-fingers specifically recognize individual bases positioned for access in otherwise intricately folded 'loop' regions of the RNA.

Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition.,Lu D, Searles MA, Klug A Nature. 2003 Nov 6;426(6962):96-100. PMID:14603324^[1]

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

References

↑ Lu D, Searles MA, Klug A. Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition. Nature. 2003 Nov 6;426(6962):96-100. PMID:14603324 doi:10.1038/nature02088

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1un6"

@@ Line 3: / Line 3: @@
 <StructureSection load='1un6' size='340' side='right'caption='[[1un6]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1un6]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/African_clawed_frog African clawed frog] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. The March 2007 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Zinc Fingers''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2007_3 10.2210/rcsb_pdb/mom_2007_3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UN6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1un6]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. The March 2007 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Zinc Fingers''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2007_3 10.2210/rcsb_pdb/mom_2007_3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UN6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tf3|1tf3]], [[1tf6|1tf6]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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=1un6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1un6 OCA], [https://pdbe.org/1un6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1un6 RCSB], [https://www.ebi.ac.uk/pdbsum/1un6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1un6 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/TF3A_XENLA TF3A_XENLA] Acts as both a positive transcription factor for 5S RNA genes and a specific RNA binding protein that complexes with 5S RNA in oocytes to form the 7S ribonucleoprotein storage particle. May play an essential role in the developmental change in 5S RNA gene expression. Interacts with the internal control region (ICR) of approximately 50 bases within the 5S RNA genes, is required for correct transcription of these genes by RNA polymerase III. Also binds the transcribed 5S RNA's.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: African clawed frog]]
 [[Category: Large Structures]]
 [[Category: RCSB PDB Molecule of the Month]]
 [[Category: Xenopus laevis]]
 [[Category: Zinc Fingers]]
-[[Category: Klug, A]]
+[[Category: Klug A]]
-[[Category: Lu, D]]
+[[Category: Lu D]]
-[[Category: Searles, M A]]
+[[Category: Searles MA]]
-[[Category: 5s ribosomal rna]]
-[[Category: Dna-binding]]
-[[Category: Nuclear protein]]
-[[Category: Rna-binding]]
-[[Category: Rna-binding protein-rna complex]]
-[[Category: Rna-binding protein/rna]]
-[[Category: Rna-protein complex]]
-[[Category: Tfiiia]]
-[[Category: Transcription regulation]]
-[[Category: X. laevi]]
-[[Category: Zinc finger]]

1un6

From Proteopedia

Current revision

THE CRYSTAL STRUCTURE OF A ZINC FINGER - RNA COMPLEX REVEALS TWO MODES OF MOLECULAR RECOGNITION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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