2m3x: Difference between revisions
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{{Large structure}} | |||
==Solution structure of Ph1500: a homohexameric protein centered on a 12-bladed beta-propeller== | ==Solution structure of Ph1500: a homohexameric protein centered on a 12-bladed beta-propeller== | ||
<StructureSection load='2m3x' size='340' side='right' caption='[[2m3x]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2m3x' size='340' side='right' caption='[[2m3x]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2m3x]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2m3x]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M3X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M3X FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jv2|2jv2]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jv2|2jv2]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PH1500 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70601 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PH1500 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70601 Pyrococcus horikoshii])</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=2m3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m3x OCA], [http://pdbe.org/2m3x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m3x RCSB], [http://www.ebi.ac.uk/pdbsum/2m3x PDBsum]</span></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=2m3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m3x OCA], [http://pdbe.org/2m3x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m3x RCSB], [http://www.ebi.ac.uk/pdbsum/2m3x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2m3x ProSAT]</span></td></tr> | ||
</table> | </table> | ||
{{Large structure}} | {{Large structure}} | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Pyrococcus horikoshii]] | ||
[[Category: Coles, M]] | [[Category: Coles, M]] | ||
[[Category: Kessler, H]] | [[Category: Kessler, H]] | ||
Revision as of 09:58, 18 October 2016
Solution structure of Ph1500: a homohexameric protein centered on a 12-bladed beta-propellerSolution structure of Ph1500: a homohexameric protein centered on a 12-bladed beta-propeller
Structural highlights
Warning: this is a large structure, and loading might take a long time or not happen at all. Publication Abstract from PubMedPh1500 is a homohexameric, two-domain protein of unknown function from the hyperthermophilic archaeon Pyrococcus horikoshii. The C-terminal hexamerization domain (Ph1500C) is of particular interest, as it lacks sequence homology to proteins of known structure. However, it resisted crystallization for X-ray analysis, and proteins of this size (49 kDa) present a considerable challenge to NMR structure determination in solution. We solved the high-resolution structure of Ph1500C, exploiting the hyperthermophilic nature of the protein to minimize unfavorable relaxation properties by high-temperature measurement. Thus, the side chain assignment (97%) and structure determination became possible at full proton density. To our knowledge, Ph1500C is the largest protein for which this has been achieved. To minimize detrimental fast water exchange of amide protons at increased temperature, we employed a strategy where the temperature was optimized separately for backbone and side chain experiments. Optimized measurement temperature gives access to the solution structure of a 49 kDa homohexameric beta-propeller.,Varnay I, Truffault V, Djuranovic S, Ursinus A, Coles M, Kessler H J Am Chem Soc. 2010 Nov 10;132(44):15692-8. doi: 10.1021/ja1064608. PMID:20961124[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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