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3k64

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Revision as of 09:22, 26 December 2018

Crystal structure of FBF-2/fem-3 PME complex

Structural highlights

3k64 is a 2 chain structure with sequence from Caeel. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3k5q, 3k5y, 3k5z, 3k61, 3k62
Gene:	F21H12.5, fbf-2 (CAEEL)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FBF2_CAEEL] Involved in the control of stem cells and sex determination in the C.elegans hermaphrodite germline. May also play a role in the hermaphrodite germline proliferation and oogenesis. Binds specifically to the regulatory region of fem-3 3'-UTR and mediates the sperm/oocyte switch. Negatively regulates gld-3 expression possibly by directly binding to two sites within the gld-3 isoform B 3'-UTR.^[1] ^[2]

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

Caenorhabditis elegans fem-3 binding factor (FBF) is a founding member of the PUMILIO/FBF (PUF) family of mRNA regulatory proteins. It regulates multiple mRNAs critical for stem cell maintenance and germline development. Here, we report crystal structures of FBF in complex with 6 different 9-nt RNA sequences, including elements from 4 natural mRNAs. These structures reveal that FBF binds to conserved bases at positions 1-3 and 7-8. The key specificity determinant of FBF vs. other PUF proteins lies in positions 4-6. In FBF/RNA complexes, these bases stack directly with one another and turn away from the RNA-binding surface. A short region of FBF is sufficient to impart its unique specificity and lies directly opposite the flipped bases. We suggest that this region imposes a flattened curvature on the protein; hence, the requirement for the additional nucleotide. The principles of FBF/RNA recognition suggest a general mechanism by which PUF proteins recognize distinct families of RNAs yet exploit very nearly identical atomic contacts in doing so.

Structural basis for specific recognition of multiple mRNA targets by a PUF regulatory protein.,Wang Y, Opperman L, Wickens M, Hall TM Proc Natl Acad Sci U S A. 2009 Dec 1;106(48):20186-91. Epub 2009 Nov 9. PMID:19901328^[3]

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

References

↑ Zhang B, Gallegos M, Puoti A, Durkin E, Fields S, Kimble J, Wickens MP. A conserved RNA-binding protein that regulates sexual fates in the C. elegans hermaphrodite germ line. Nature. 1997 Dec 4;390(6659):477-84. PMID:9393998 doi:10.1038/37297
↑ Eckmann CR, Crittenden SL, Suh N, Kimble J. GLD-3 and control of the mitosis/meiosis decision in the germline of Caenorhabditis elegans. Genetics. 2004 Sep;168(1):147-60. PMID:15454534 doi:10.1534/genetics.104.029264
↑ Wang Y, Opperman L, Wickens M, Hall TM. Structural basis for specific recognition of multiple mRNA targets by a PUF regulatory protein. Proc Natl Acad Sci U S A. 2009 Dec 1;106(48):20186-91. Epub 2009 Nov 9. PMID:19901328

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/3k64"

@@ Line 1: / Line 1: @@
 ==Crystal structure of FBF-2/fem-3 PME complex==
 <StructureSection load='3k64' size='340' side='right' caption='[[3k64]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3k5q|3k5q]], [[3k5y|3k5y]], [[3k5z|3k5z]], [[3k61|3k61]], [[3k62|3k62]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">F21H12.5, fbf-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=3k64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k64 OCA], [http://pdbe.org/3k64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k64 RCSB], [http://www.ebi.ac.uk/pdbsum/3k64 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=3k64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k64 OCA], [http://pdbe.org/3k64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k64 RCSB], [http://www.ebi.ac.uk/pdbsum/3k64 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k64 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k6/3k64_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k6/3k64_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

3k64

From Proteopedia

Revision as of 09:22, 26 December 2018

Crystal structure of FBF-2/fem-3 PME complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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