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| | ==Crystal structure of APE1850== | | ==Crystal structure of APE1850== |
| - | <StructureSection load='2cy1' size='340' side='right' caption='[[2cy1]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='2cy1' size='340' side='right'caption='[[2cy1]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2cy1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aerpe Aerpe]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CY1 FirstGlance]. <br> | + | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cy1 OCA], [http://pdbe.org/2cy1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cy1 RCSB], [http://www.ebi.ac.uk/pdbsum/2cy1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cy1 ProSAT], [http://www.topsan.org/Proteins/RSGI/2cy1 TOPSAN]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9YAU4_AERPE Q9YAU4_AERPE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aerpe]] | + | [[Category: Aeropyrum pernix K1]] |
| - | [[Category: Bessho, Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]] | + | [[Category: Bessho Y]] |
| - | [[Category: Shibata, R]] | + | [[Category: Shibata R]] |
| - | [[Category: Shirouzu, M]] | + | [[Category: Shirouzu M]] |
| - | [[Category: Umehara, T]] | + | [[Category: Umehara T]] |
| - | [[Category: Yokoyama, S]] | + | [[Category: Yokoyama S]] |
| - | [[Category: Archaeal nusa]]
| + | |
| - | [[Category: Kh domain]]
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| - | [[Category: Microgravity]]
| + | |
| - | [[Category: National project on protein structural and functional analyse]]
| + | |
| - | [[Category: Nppsfa]]
| + | |
| - | [[Category: Rna binding protein]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription termination]]
| + | |
| Structural highlights
Function
Q9YAU4_AERPE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. Crystallization of the archaeal transcription termination factor NusA: a significant decrease in twinning under microgravity conditions. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Feb 1;63(Pt, 2):69-73. Epub 2007 Jan 17. PMID:17277442 doi:http://dx.doi.org/10.1107/S1744309106054625
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