1p5s

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(New page: 200px<br /><applet load="1p5s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p5s, resolution 2.22&Aring;" /> '''STRUCTURE AND FUNCTI...)
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[[Image:1p5s.jpg|left|200px]]<br /><applet load="1p5s" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1p5s, resolution 2.22&Aring;" />
 
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'''STRUCTURE AND FUNCTION OF THE CALPONIN-HOMOLOGY DOMAIN OF AN IQGAP PROTEIN FROM SCHIZOSACCHAROMYCES POMBE'''<br />
 
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==Overview==
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==STRUCTURE AND FUNCTION OF THE CALPONIN-HOMOLOGY DOMAIN OF AN IQGAP PROTEIN FROM SCHIZOSACCHAROMYCES POMBE==
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Schizosaccharomyces pombe Rng2 is an IQGAP protein that is essential for, the assembly of an actomyosin ring during cytokinesis. Rng2 contains an, amino-terminal calponin-homology (CH) domain, 11 IQ repeats and a, RasGAP-homology domain. CH domains are known mainly for their ability to, bind F-actin, although they have other ligands in vivo and there are only, few examples of actin-binding single CH domains. The structures of several, CH domains have already been reported, but this is only the third report, of an actin-binding protein that contains a single CH domain (the, structures of calponin and EB1 have been reported previously). The 2.21 A, resolution crystal structure of the amino-terminal 190 residues of Rng2, from Br- and Hg-derivatives includes 40 residues (150-190), carboxyl-terminal to the CH domain that resemble neither the extended, conformation seen in utrophin, nor the compact conformation seen in, fimbrin, although residues 154-160 form an unstructured coil which adopts, a substructure similar to dystrophin residues 240-246 in the, carboxyl-terminal portion of the CH2 domain. This region wraps around the, stretch of residues that would be equivalent to the proposed actin-binding, site ABS1 and ABS2 from dystrophin. This distinctive feature is absent, from previously published CH-domain structures. Another feature revealed, by comparing the two derivatives is the presence of two loop conformations, between Tyr92 and Arg99.
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<StructureSection load='1p5s' size='340' side='right'caption='[[1p5s]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1p5s]] is a 1 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=1P5S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P5S FirstGlance]. <br>
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1P5S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe] with HG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P5S OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.22&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5s OCA], [https://pdbe.org/1p5s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p5s RCSB], [https://www.ebi.ac.uk/pdbsum/1p5s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p5s ProSAT]</span></td></tr>
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Structure, crystal packing and molecular dynamics of the calponin-homology domain of Schizosaccharomyces pombe Rng2., Wang CH, Balasubramanian MK, Dokland T, Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1396-403. Epub 2004, Jul 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15272162 15272162]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RNG2_SCHPO RNG2_SCHPO] Required for cytokinesis. Component of the contractile F-actin ring; required for its construction following assembly of F-actin at the division site.<ref>PMID:9635188</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p5/1p5s_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1p5s ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Schizosaccharomyces pombe]]
[[Category: Schizosaccharomyces pombe]]
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[[Category: Single protein]]
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[[Category: Balasubramanian MK]]
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[[Category: Balasubramanian, M.K.]]
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[[Category: Dokland T]]
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[[Category: Dokland, T.]]
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[[Category: Wang CH]]
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[[Category: Wang, C.H.]]
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[[Category: HG]]
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[[Category: alpha-helical bundle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:29:44 2007''
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Current revision

STRUCTURE AND FUNCTION OF THE CALPONIN-HOMOLOGY DOMAIN OF AN IQGAP PROTEIN FROM SCHIZOSACCHAROMYCES POMBE

PDB ID 1p5s

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