View source for 3qtb


==Structure of the universal stress protein from Archaeoglobus fulgidus in complex with dAMP==
<StructureSection load='3qtb' size='340' side='right'caption='[[3qtb]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3qtb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QTB 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=D5M:2-DEOXYADENOSINE-5-MONOPHOSPHATE'>D5M</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=3qtb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qtb OCA], [https://pdbe.org/3qtb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qtb RCSB], [https://www.ebi.ac.uk/pdbsum/3qtb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qtb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O29432_ARCFU O29432_ARCFU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We 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<ref>PMID:23745136</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qtb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Archaeoglobus fulgidus]]
[[Category: Large Structures]]
[[Category: Chruszcz M]]
[[Category: Cymborowski M]]
[[Category: Di Leo R]]
[[Category: Joachimiak A]]
[[Category: Minor W]]
[[Category: Savchenko A]]
[[Category: Shumilin IA]]
[[Category: Tkaczuk KL]]
[[Category: Xu X]]