2v52: Difference between revisions

Revision as of 00:59, 2 October 2014

STRUCTURE OF MAL-RPEL2 COMPLEXED TO G-ACTIN

Structural highlights

2v52 is a 2 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	ATP, GOL, LAB, MG
Related:	1lcu, 2a42, 2aso, 1ijj, 1wua, 1o18, 1m8q, 1o1a, 1rfq, 1uy5, 1ma9, 2d1k, 1rdw, 1o1b, 1o1d, 2a40, 2a5x, 1qz5, 1nwk, 1j6z, 1sqk, 1atn, 1s22, 1t44, 2ff3, 1eqy, 1mvw, 2ff6, 2fxu, 1o1f, 1kxp, 2asp, 1rgi, 1o19, 1y64, 1alm, 1o1e, 1esv, 1p8z, 1h1v, 1o1c, 2vcp, 1o1g, 2a3z, 1lot, 2asm, 2a41, 2vyp, 1qz6, 2v51
Resources:	FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

Serum response factor transcriptional activity is controlled through interactions with regulatory cofactors such as the coactivator MAL/MRTF-A (myocardin-related transcription factor A). MAL is itself regulated in vivo by changes in cellular actin dynamics, which alter its interaction with G-actin. The G-actin-sensing mechanism of MAL/MRTF-A resides in its N-terminal domain, which consists of three tandem RPEL repeats. We describe the first molecular insights into RPEL function obtained from structures of two independent RPEL(MAL) peptide:G-actin complexes. Both RPEL peptides bind to the G-actin hydrophobic cleft and to subdomain 3. These RPEL(MAL):G-actin structures explain the sequence conservation defining the RPEL motif, including the invariant arginine. Characterisation of the RPEL(MAL):G-actin interaction by fluorescence anisotropy and cell reporter-based assays validates the significance of actin-binding residues for proper MAL localisation and regulation in vivo. We identify important differences in G-actin engagement between the two RPEL(MAL) structures. Comparison with other actin-binding proteins reveals an unexpected similarity to the vitamin-D-binding protein, extending the G-actin-binding protein repertoire.

Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL.,Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ EMBO J. 2008 Nov 13. PMID:19008859^[1]

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

References

↑ Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ. Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. EMBO J. 2008 Nov 13. PMID:19008859 doi:emboj2008235

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OCA

[1] Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ. Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. EMBO J. 2008 Nov 13. PMID:19008859 doi:emboj2008235

[1]

@@ Line 1: / Line 1: @@
-[[Image:2v52.png|left|200px]]
+==STRUCTURE OF MAL-RPEL2 COMPLEXED TO G-ACTIN==
+<StructureSection load='2v52' size='340' side='right' caption='[[2v52]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2v52]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V52 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LAB:LATRUNCULIN+B'>LAB</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lcu|1lcu]], [[2a42|2a42]], [[2aso|2aso]], [[1ijj|1ijj]], [[1wua|1wua]], [[1o18|1o18]], [[1m8q|1m8q]], [[1o1a|1o1a]], [[1rfq|1rfq]], [[1uy5|1uy5]], [[1ma9|1ma9]], [[2d1k|2d1k]], [[1rdw|1rdw]], [[1o1b|1o1b]], [[1o1d|1o1d]], [[2a40|2a40]], [[2a5x|2a5x]], [[1qz5|1qz5]], [[1nwk|1nwk]], [[1j6z|1j6z]], [[1sqk|1sqk]], [[1atn|1atn]], [[1s22|1s22]], [[1t44|1t44]], [[2ff3|2ff3]], [[1eqy|1eqy]], [[1mvw|1mvw]], [[2ff6|2ff6]], [[2fxu|2fxu]], [[1o1f|1o1f]], [[1kxp|1kxp]], [[2asp|2asp]], [[1rgi|1rgi]], [[1o19|1o19]], [[1y64|1y64]], [[1alm|1alm]], [[1o1e|1o1e]], [[1esv|1esv]], [[1p8z|1p8z]], [[1h1v|1h1v]], [[1o1c|1o1c]], [[2vcp|2vcp]], [[1o1g|1o1g]], [[2a3z|2a3z]], [[1lot|1lot]], [[2asm|2asm]], [[2a41|2a41]], [[2vyp|2vyp]], [[1qz6|1qz6]], [[2v51|2v51]]</td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v52 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v52 RCSB], [http://www.ebi.ac.uk/pdbsum/2v52 PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Serum response factor transcriptional activity is controlled through interactions with regulatory cofactors such as the coactivator MAL/MRTF-A (myocardin-related transcription factor A). MAL is itself regulated in vivo by changes in cellular actin dynamics, which alter its interaction with G-actin. The G-actin-sensing mechanism of MAL/MRTF-A resides in its N-terminal domain, which consists of three tandem RPEL repeats. We describe the first molecular insights into RPEL function obtained from structures of two independent RPEL(MAL) peptide:G-actin complexes. Both RPEL peptides bind to the G-actin hydrophobic cleft and to subdomain 3. These RPEL(MAL):G-actin structures explain the sequence conservation defining the RPEL motif, including the invariant arginine. Characterisation of the RPEL(MAL):G-actin interaction by fluorescence anisotropy and cell reporter-based assays validates the significance of actin-binding residues for proper MAL localisation and regulation in vivo. We identify important differences in G-actin engagement between the two RPEL(MAL) structures. Comparison with other actin-binding proteins reveals an unexpected similarity to the vitamin-D-binding protein, extending the G-actin-binding protein repertoire.
-{{STRUCTURE_2v52|  PDB=2v52  |  SCENE=  }}
+Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL.,Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ EMBO J. 2008 Nov 13. PMID:19008859<ref>PMID:19008859</ref>
-===STRUCTURE OF MAL-RPEL2 COMPLEXED TO G-ACTIN===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_19008859}}
-==About this Structure==
-[[2v52]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V52 OCA].
 ==See Also==
 *[[Actin|Actin]]
+*[[Transcriptional activator|Transcriptional activator]]
-==Reference==
+== References ==
-<ref group="xtra">PMID:019008859</ref><references group="xtra"/>
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Oryctolagus cuniculus]]
 [[Category: Guettler, S.]]

2v52: Difference between revisions

Revision as of 00:59, 2 October 2014

STRUCTURE OF MAL-RPEL2 COMPLEXED TO G-ACTIN

Structural highlights

Publication Abstract from PubMed

See Also

References

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