1yrg: Difference between revisions

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New page: left|200px<br /><applet load="1yrg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yrg, resolution 2.66Å" /> '''THE CRYSTAL STRUCTUR...
 
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[[Image:1yrg.gif|left|200px]]<br /><applet load="1yrg" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1yrg, resolution 2.66&Aring;" />
'''THE CRYSTAL STRUCTURE OF RNA1P: A NEW FOLD FOR A GTPASE-ACTIVATING PROTEIN'''<br />


==Overview==
==THE CRYSTAL STRUCTURE OF RNA1P: A NEW FOLD FOR A GTPASE-ACTIVATING PROTEIN==
rna1p is the Schizosaccharomyces pombe ortholog of the mammalian, GTPase-activating protein (GAP) of Ran. Both proteins are essential for, nuclear transport. Here, we report the crystal structure of rna1p at 2.66, A resolution. It contains 11 leucine-rich repeats that adopt the, nonglobular shape of a crescent, bearing no resemblance to RhoGAP or, RasGAP. The invariant residues of RanGAP form a contiguous surface, strongly indicating the Ran-binding interface. Alanine mutations identify, Arg-74 as a critical residue for GTP hydrolysis. In contrast to RasGAP and, RhoGAP, Arg-74 could be substituted by lysine and contributed, significantly to the binding of Ran. Therefore, we suggest a GAP mechanism, for rna1p, which constitutes a variation of the arginine finger mechanism, found for Ras GAP and RhoGAP.
<StructureSection load='1yrg' size='340' side='right'caption='[[1yrg]], [[Resolution|resolution]] 2.66&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1yrg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YRG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.66&#8491;</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=1yrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yrg OCA], [https://pdbe.org/1yrg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yrg RCSB], [https://www.ebi.ac.uk/pdbsum/1yrg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yrg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RNA1_SCHPO RNA1_SCHPO] GTPase activator for the nuclear Ras-related regulatory protein spi1 (Ran), converting it to the putatively inactive GDP-bound state.
== 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/yr/1yrg_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=1yrg ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
rna1p is the Schizosaccharomyces pombe ortholog of the mammalian GTPase-activating protein (GAP) of Ran. Both proteins are essential for nuclear transport. Here, we report the crystal structure of rna1p at 2.66 A resolution. It contains 11 leucine-rich repeats that adopt the nonglobular shape of a crescent, bearing no resemblance to RhoGAP or RasGAP. The invariant residues of RanGAP form a contiguous surface, strongly indicating the Ran-binding interface. Alanine mutations identify Arg-74 as a critical residue for GTP hydrolysis. In contrast to RasGAP and RhoGAP, Arg-74 could be substituted by lysine and contributed significantly to the binding of Ran. Therefore, we suggest a GAP mechanism for rna1p, which constitutes a variation of the arginine finger mechanism found for Ras GAP and RhoGAP.


==About this Structure==
The crystal structure of rna1p: a new fold for a GTPase-activating protein.,Hillig RC, Renault L, Vetter IR, Drell T 4th, Wittinghofer A, Becker J Mol Cell. 1999 Jun;3(6):781-91. PMID:10394366<ref>PMID:10394366</ref>
1YRG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YRG OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The crystal structure of rna1p: a new fold for a GTPase-activating protein., Hillig RC, Renault L, Vetter IR, Drell T 4th, Wittinghofer A, Becker J, Mol Cell. 1999 Jun;3(6):781-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10394366 10394366]
</div>
<div class="pdbe-citations 1yrg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Schizosaccharomyces pombe]]
[[Category: Schizosaccharomyces pombe]]
[[Category: Single protein]]
[[Category: Becker J]]
[[Category: Becker, J.]]
[[Category: Drell T]]
[[Category: Drell, T.]]
[[Category: Hillig RC]]
[[Category: Hillig, R.C.]]
[[Category: Renault L]]
[[Category: Renault, L.]]
[[Category: Vetter IR]]
[[Category: Vetter, I.R.]]
[[Category: Wittinghofer A]]
[[Category: Wittinghofer, A.]]
[[Category: gap]]
[[Category: gtpase-activating protein]]
[[Category: hemihedral twinning]]
[[Category: leucine-rich repeat protein]]
[[Category: lrr]]
[[Category: merohedral twinning]]
[[Category: merohedry]]
[[Category: rangap]]
[[Category: rna1p]]
[[Category: twinning]]
 
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