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[[Image:2chd.gif|left|200px]]
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{{STRUCTURE_2chd|  PDB=2chd  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF THE C2A DOMAIN OF RABPHILIN-3A'''


==Crystal structure of the C2A domain of Rabphilin-3A==
<StructureSection load='2chd' size='340' side='right'caption='[[2chd]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2chd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CHD 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]] 1.92&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2chd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2chd OCA], [https://pdbe.org/2chd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2chd RCSB], [https://www.ebi.ac.uk/pdbsum/2chd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2chd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RP3A_RAT RP3A_RAT] Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal.
== 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/ch/2chd_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=2chd ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rabphilin-3A is a neuronal protein containing a C2-domain tandem. To date, only the structure of the C2B domain has been solved. The crystal structure of the Ca2+-free C2A domain has been solved by molecular replacement and refined to 1.92 A resolution. It adopts the classical C2-domain fold consisting of an eight-stranded antiparallel beta-sandwich with type I topology. In agreement with its Ca2+-dependent negatively charged membrane-binding properties, this C2 domain contains all the conserved acidic residues responsible for calcium binding. However, the replacement of a conserved aspartic acid residue by glutamic acid allows formation of an additional strong hydrogen bond, resulting in increased rigidity of calcium-binding loop 1. The electrostatic surface of the C2A domain consists of a large positively charged belt surrounded by two negatively charged patches located at both tips of the domain. In comparison, the structurally very similar C2A domain of synaptotagmin I has a highly acidic electrostatic surface, suggesting completely unrelated functions for these two C2A domains.


==Overview==
Structure of the C2A domain of rabphilin-3A.,Biadene M, Montaville P, Sheldrick GM, Becker S Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):793-9. Epub 2006, Jun 20. PMID:16790935<ref>PMID:16790935</ref>
Rabphilin-3A is a neuronal protein containing a C2-domain tandem. To date, only the structure of the C2B domain has been solved. The crystal structure of the Ca2+-free C2A domain has been solved by molecular replacement and refined to 1.92 A resolution. It adopts the classical C2-domain fold consisting of an eight-stranded antiparallel beta-sandwich with type I topology. In agreement with its Ca2+-dependent negatively charged membrane-binding properties, this C2 domain contains all the conserved acidic residues responsible for calcium binding. However, the replacement of a conserved aspartic acid residue by glutamic acid allows formation of an additional strong hydrogen bond, resulting in increased rigidity of calcium-binding loop 1. The electrostatic surface of the C2A domain consists of a large positively charged belt surrounded by two negatively charged patches located at both tips of the domain. In comparison, the structurally very similar C2A domain of synaptotagmin I has a highly acidic electrostatic surface, suggesting completely unrelated functions for these two C2A domains.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2CHD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHD OCA].
</div>
<div class="pdbe-citations 2chd" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure of the C2A domain of rabphilin-3A., Biadene M, Montaville P, Sheldrick GM, Becker S, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):793-9. Epub 2006, Jun 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16790935 16790935]
*[[Exophilin 3D structures|Exophilin 3D structures]]
*[[Rabphilin|Rabphilin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Becker S]]
[[Category: Becker, S.]]
[[Category: Biadene M]]
[[Category: Biadene, M.]]
[[Category: Montaville P]]
[[Category: Montaville, P.]]
[[Category: Sheldrick GM]]
[[Category: Sheldrick, G M.]]
[[Category: C2 domain]]
[[Category: C2a]]
[[Category: Calcium binding]]
[[Category: Metal-binding]]
[[Category: Protein transport]]
[[Category: Rabphilin-3a]]
[[Category: Synapse]]
[[Category: Synaptic exocytosis]]
[[Category: Transport]]
[[Category: Zinc]]
[[Category: Zinc-finger]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 22:08:41 2008''