View source for 2cy1


==Crystal structure of APE1850==
<StructureSection load='2cy1' size='340' side='right'caption='[[2cy1]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2cy1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeropyrum_pernix_K1 Aeropyrum pernix K1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CY1 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]] 2.3&#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=2cy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cy1 OCA], [https://pdbe.org/2cy1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cy1 RCSB], [https://www.ebi.ac.uk/pdbsum/2cy1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cy1 ProSAT], [https://www.topsan.org/Proteins/RSGI/2cy1 TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9YAU4_AERPE Q9YAU4_AERPE] 
== 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/cy/2cy1_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=2cy1 ConSurf].
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== Publication Abstract from PubMed ==
The transcription termination factor NusA from Aeropyrum pernix was crystallized using a counter-diffusion technique in both terrestrial and microgravity environments. Crystallization under microgravity conditions significantly reduced the twinning content (1.0%) compared with terrestrially grown crystals (18.3%) and improved the maximum resolution from 3.0 to 2.29 A, with similar unit-cell parameters. Based on a comparison of the crystal parameters, the effect of microgravity on protein crystallization is discussed.

Crystallization of the archaeal transcription termination factor NusA: a significant decrease in twinning under microgravity conditions.,Tanaka H, Umehara T, Inaka K, Takahashi S, Shibata R, Bessho Y, Sato M, Sugiyama S, Fusatomi E, Terada T, Shirouzu M, Sano S, Motohara M, Kobayashi T, Tanaka T, Tanaka A, Yokoyama S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Feb 1;63(Pt, 2):69-73. Epub 2007 Jan 17. PMID:17277442<ref>PMID:17277442</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2cy1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aeropyrum pernix K1]]
[[Category: Large Structures]]
[[Category: Bessho Y]]
[[Category: Shibata R]]
[[Category: Shirouzu M]]
[[Category: Umehara T]]
[[Category: Yokoyama S]]