View source for 2dcp


==Fully automated NMR structure determination of the ENTH-VHS domain AT3G16270 from Arabidopsis thaliana==
<StructureSection load='2dcp' size='340' side='right'caption='[[2dcp]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2dcp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DCP 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=2dcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dcp OCA], [https://pdbe.org/2dcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dcp RCSB], [https://www.ebi.ac.uk/pdbsum/2dcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dcp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MTV1_ARATH MTV1_ARATH] Mediates clathrin-dependent trafficking of vacuolar cargo from the trans-Golgi network (TGN). Promotes plant growth.<ref>PMID:23771894</ref> 
== 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/dc/2dcp_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=2dcp ConSurf].
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== Publication Abstract from PubMed ==
Fully automated structure determination of proteins in solution (FLYA) yields, without human intervention, three-dimensional protein structures starting from a set of multidimensional NMR spectra. Integrating existing and new software, automated peak picking over all spectra is followed by peak list filtering, the generation of an ensemble of initial chemical shift assignments, the determination of consensus chemical shift assignments for all (1)H, (13)C, and (15)N nuclei, the assignment of NOESY cross-peaks, the generation of distance restraints, and the calculation of the three-dimensional structure by torsion angle dynamics. The resulting, preliminary structure serves as additional input to the second stage of the procedure, in which a new ensemble of chemical shift assignments and a refined structure are calculated. The three-dimensional structures of three 12-16 kDa proteins computed with the FLYA algorithm coincided closely with the conventionally determined structures. Deviations were below 0.95 A for the backbone atom positions, excluding the flexible chain termini. 96-97% of all backbone and side-chain chemical shifts in the structured regions were assigned to the correct residues. The purely computational FLYA method is suitable for substituting all manual spectra analysis and thus overcomes a main efficiency limitation of the NMR method for protein structure determination.

Automated protein structure determination from NMR spectra.,Lopez-Mendez B, Guntert P J Am Chem Soc. 2006 Oct 11;128(40):13112-22. PMID:17017791<ref>PMID:17017791</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Guntert P]]
[[Category: Lopez-Mendez B]]