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| | <StructureSection load='1x6x' size='340' side='right'caption='[[1x6x]], [[Resolution|resolution]] 0.96Å' scene=''> | | <StructureSection load='1x6x' size='340' side='right'caption='[[1x6x]], [[Resolution|resolution]] 0.96Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1x6x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X6X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1X6X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1x6x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X6X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X6X FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dzo|1dzo]], [[1x6p|1x6p]], [[1x6q|1x6q]], [[1x6r|1x6r]], [[1x6y|1x6y]], [[1x6z|1x6z]]</div></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]] 0.96Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pilA, fimA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=1x6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x6x OCA], [https://pdbe.org/1x6x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x6x RCSB], [https://www.ebi.ac.uk/pdbsum/1x6x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x6x ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1x6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x6x OCA], [http://pdbe.org/1x6x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x6x RCSB], [http://www.ebi.ac.uk/pdbsum/1x6x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1x6x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FMPA_PSEAI FMPA_PSEAI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dunlop, K V]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Hazes, B]] | + | [[Category: Dunlop KV]] |
| - | [[Category: Irvin, R T]] | + | [[Category: Hazes B]] |
| - | [[Category: Adhesin]] | + | [[Category: Irvin RT]] |
| - | [[Category: Lectin]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| - | [[Category: Type iv pilin]]
| + | |
| Structural highlights
Function
FMPA_PSEAI
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
High-resolution protein structures are becoming more common owing to the availability of increasingly brilliant synchrotron X-ray sources. However, to withstand the increased X-ray dose the crystals must be held at cryogenic temperatures. To compare the benefit of increased resolution with the drawback of potential temperature-induced changes, three room-temperature and three cryogenic data sets for PAK pilin have been collected at resolutions between 1.8 and 0.78 A. The results show that although the high-resolution cryogenic structures are more precise and more detailed, they also show systematic deviations from the room-temperature structures. Small but significant differences are even observed in the structural core, whilst more extensive changes occur at the protein surface. These differences can affect biological interpretations, especially because many important biological processes take place at the protein surface. Accordingly, although high-quality cryogenic synchrotron data is extremely valuable to protein crystallography, room-temperature structures are still desirable, especially if the research question involves protein features that are sensitive to temperature-induced changes.
Pros and cons of cryocrystallography: should we also collect a room-temperature data set?,Dunlop KV, Irvin RT, Hazes B Acta Crystallogr D Biol Crystallogr. 2005 Jan;61(Pt 1):80-7. Epub 2004 Dec, 17. PMID:15608379[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dunlop KV, Irvin RT, Hazes B. Pros and cons of cryocrystallography: should we also collect a room-temperature data set? Acta Crystallogr D Biol Crystallogr. 2005 Jan;61(Pt 1):80-7. Epub 2004 Dec, 17. PMID:15608379 doi:10.1107/S0907444904027179
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