1rh8: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1rh8.jpg|left|200px]]<br /><applet load="1rh8" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1rh8" />
-'''Three-dimensional structure of the calcium-free Piccolo C2A-domain'''<br />
-==Overview==
+==Three-dimensional structure of the calcium-free Piccolo C2A-domain==
-C2 domains are widespread Ca2+-binding modules. The active zone protein, Piccolo (also known as Aczonin) contains an unusual C2A domain that, exhibits a low affinity for Ca2+, a Ca2+-induced conformational change and, Ca2+-dependent dimerization. We show here that removal of a nine-residue, sequence by alternative splicing increases the Ca2+ affinity, abolishes, the conformational change and abrogates dimerization of the Piccolo C2A, domain. The NMR structure of the Ca2+-free long variant provides a, structural basis for these different properties of the two splice forms, showing that the nine-residue sequence forms a beta-strand otherwise, occupied by a nonspliced sequence. Consequently, Ca2+-binding to the long, Piccolo C2A domain requires a marked rearrangement of secondary structure, that cannot occur for the short variant. These results reveal a novel, mechanism of action of C2 domains and uncover a structural principle that, may underlie the alteration of protein function by short alternatively, spliced sequences.
+<StructureSection load='1rh8' size='340' side='right'caption='[[1rh8]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1rh8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RH8 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1rh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rh8 OCA], [https://pdbe.org/1rh8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rh8 RCSB], [https://www.ebi.ac.uk/pdbsum/1rh8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rh8 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PCLO_RAT PCLO_RAT] May act as a scaffolding protein involved in the organization of synaptic active zones and in synaptic vesicle trafficking (By similarity).[UniProtKB:Q9QYX7]
+== 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/rh/1rh8_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=1rh8 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+C2 domains are widespread Ca2+-binding modules. The active zone protein Piccolo (also known as Aczonin) contains an unusual C2A domain that exhibits a low affinity for Ca2+, a Ca2+-induced conformational change and Ca2+-dependent dimerization. We show here that removal of a nine-residue sequence by alternative splicing increases the Ca2+ affinity, abolishes the conformational change and abrogates dimerization of the Piccolo C2A domain. The NMR structure of the Ca2+-free long variant provides a structural basis for these different properties of the two splice forms, showing that the nine-residue sequence forms a beta-strand otherwise occupied by a nonspliced sequence. Consequently, Ca2+-binding to the long Piccolo C2A domain requires a marked rearrangement of secondary structure that cannot occur for the short variant. These results reveal a novel mechanism of action of C2 domains and uncover a structural principle that may underlie the alteration of protein function by short alternatively spliced sequences.
-==About this Structure==
+A conformational switch in the Piccolo C2A domain regulated by alternative splicing.,Garcia J, Gerber SH, Sugita S, Sudhof TC, Rizo J Nat Struct Mol Biol. 2004 Jan;11(1):45-53. Epub 2003 Dec 29. PMID:14718922<ref>PMID:14718922</ref>
-RH8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RH8 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-A conformational switch in the Piccolo C2A domain regulated by alternative splicing., Garcia J, Gerber SH, Sugita S, Sudhof TC, Rizo J, Nat Struct Mol Biol. 2004 Jan;11(1):45-53. Epub 2003 Dec 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14718922 14718922]
+</div>
+<div class="pdbe-citations 1rh8" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Rattus norvegicus]]
-[[Category: Single protein]]
+[[Category: Garcia J]]
-[[Category: Garcia, J.]]
+[[Category: Gerber SH]]
-[[Category: Gerber, S.H.]]
+[[Category: Rizo J]]
-[[Category: Rizo, J.]]
+[[Category: Sudhof TC]]
-[[Category: Sudhof, T.C.]]
+[[Category: Sugita S]]
-[[Category: Sugita, S.]]
-[[Category: beta-sandwich]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:35:50 2007''