2pfs: Difference between revisions
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==Crystal structure of universal stress protein from Nitrosomonas europaea== | ==Crystal structure of universal stress protein from Nitrosomonas europaea== | ||
<StructureSection load='2pfs' size='340' side='right' caption='[[2pfs]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='2pfs' size='340' side='right'caption='[[2pfs]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2pfs]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2pfs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Niteu Niteu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PFS FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NE1028 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NE1028 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=228410 NITEU])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pfs OCA], [https://pdbe.org/2pfs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pfs RCSB], [https://www.ebi.ac.uk/pdbsum/2pfs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pfs ProSAT], [https://www.topsan.org/Proteins/MCSG/2pfs TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Niteu]] | [[Category: Niteu]] | ||
[[Category: Chruszcz, M]] | [[Category: Chruszcz, M]] | ||
Latest revision as of 18:22, 17 June 2021
Crystal structure of universal stress protein from Nitrosomonas europaeaCrystal structure of universal stress protein from Nitrosomonas europaea
Structural highlights
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 PubMedWe present the crystal structures of two universal stress proteins (USP) from Archaeoglobus fulgidus and Nitrosomonas europaea in both apo- and ligand-bound forms. This work is the first complete synthesis of the structural properties of 26 USP available in the Protein Data Bank, over 75% of which were determined by structure genomics centers with no additional information provided. The results of bioinformatic analyses of all available USP structures and their sequence homologs revealed that these two new USP structures share overall structural similarity with structures of USPs previously determined. Clustering and cladogram analyses, however, show how they diverge from other members of the USP superfamily and show greater similarity to USPs from organisms inhabiting extreme environments. We compared them with other archaeal and bacterial USPs and discuss their similarities and differences in context of structure, sequential motifs, and potential function. We also attempted to group all analyzed USPs into families, so that assignment of the potential function to those with no experimental data available would be possible by extrapolation. Structural and functional insight into the universal stress protein family.,Tkaczuk KL, A Shumilin I, Chruszcz M, Evdokimova E, Savchenko A, Minor W Evol Appl. 2013 Apr;6(3):434-49. doi: 10.1111/eva.12057. Epub 2013 Mar 13. PMID:23745136[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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