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New page: left|200px<br /><applet load="1s0p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s0p, resolution 1.4Å" /> '''Structure of the N-Te...
 
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[[Image:1s0p.jpg|left|200px]]<br /><applet load="1s0p" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1s0p, resolution 1.4&Aring;" />
'''Structure of the N-Terminal Domain of the Adenylyl Cyclase-Associated Protein (CAP) from Dictyostelium discoideum.'''<br />


==Overview==
==Structure of the N-Terminal Domain of the Adenylyl Cyclase-Associated Protein (CAP) from Dictyostelium discoideum.==
Cyclase-associated proteins (CAPs) are widely distributed and highly, conserved proteins that regulate actin remodeling in response to cellular, signals. The N termini of CAPs play a role in Ras signaling and bind, adenylyl cyclase; the C termini bind to G-actin and thereby alter the, dynamic rearrangements of the microfilament system. We report here the, X-ray structure of the core of the N-terminal domain of the CAP from, Dictyostelium discoideum, which comprises residues 51-226, determined by a, combination of single isomorphous replacement with anomalous scattering, (SIRAS). The overall structure of this fragment is an alpha helix bundle, composed of six antiparallel helices. Results from gel filtration and, crosslinking experiments for CAP(1-226), CAP(255-464), and the full-length, protein, together with the CAP N-terminal domain structure and the, recently determined CAP C-terminal domain structure, provide evidence that, the functional structure of CAP is multimeric.
<StructureSection load='1s0p' size='340' side='right'caption='[[1s0p]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1s0p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1pn1 1pn1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S0P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S0P 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]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1s0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s0p OCA], [https://pdbe.org/1s0p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s0p RCSB], [https://www.ebi.ac.uk/pdbsum/1s0p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s0p ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAP_DICDI CAP_DICDI] May have a regulatory bifunctional role. Binds G-actin and PIP2. Involved in microfilament reorganization near the plasma membrane in a PIP2-regulated manner.
== 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/s0/1s0p_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=1s0p ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1S0P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1PN1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S0P OCA].
*[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structure of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum., Ksiazek D, Brandstetter H, Israel L, Bourenkov GP, Katchalova G, Janssen KP, Bartunik HD, Noegel AA, Schleicher M, Holak TA, Structure. 2003 Sep;11(9):1171-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12962635 12962635]
[[Category: Dictyostelium discoideum]]
[[Category: Dictyostelium discoideum]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bartunik, H.D.]]
[[Category: Bartunik HD]]
[[Category: Bourenkov, G.P.]]
[[Category: Bourenkov GP]]
[[Category: Brandstetter, H.]]
[[Category: Brandstetter H]]
[[Category: Holak, T.A.]]
[[Category: Holak TA]]
[[Category: Israel, L.]]
[[Category: Israel L]]
[[Category: Janssen, K.P.]]
[[Category: Janssen KP]]
[[Category: Katchalova, G.]]
[[Category: Katchalova G]]
[[Category: Ksiazek, D.]]
[[Category: Ksiazek D]]
[[Category: Noegel, A.A.]]
[[Category: Noegel AA]]
[[Category: Schleicher, M.]]
[[Category: Schleicher M]]
[[Category: MG]]
[[Category: alpha helix bundle]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:01:05 2007''

Latest revision as of 08:27, 14 February 2024

Structure of the N-Terminal Domain of the Adenylyl Cyclase-Associated Protein (CAP) from Dictyostelium discoideum.

1s0p, resolution 1.40Å

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