View source for 7pzo


==mite allergen Der p 3 from Dermatophagoides pteronyssinus==
<StructureSection load='7pzo' size='340' side='right'caption='[[7pzo]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7pzo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dermatophagoides_pteronyssinus Dermatophagoides pteronyssinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PZO 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]] 2.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7pzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pzo OCA], [https://pdbe.org/7pzo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pzo RCSB], [https://www.ebi.ac.uk/pdbsum/7pzo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pzo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DERP3_DERPT DERP3_DERPT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The histone-like (HU) protein is one of the major nucleoid-associated proteins of the bacterial nucleoid, which shares high sequence and structural similarity with IHF but differs from the latter in DNA-specificity. Here, we perform an analysis of structural-dynamic properties of HU protein from Spiroplasma melliferum and compare its behavior in solution to that of another mycoplasmal HU from Mycoplasma gallisepticum. The high-resolution heteronuclear NMR spectroscopy was coupled with molecular-dynamics study and comparative analysis of thermal denaturation of both mycoplasmal HU proteins. We suggest that stacking interactions in two aromatic clusters in the HUSpm dimeric interface determine not only high thermal stability of the protein, but also its structural plasticity experimentally observed as slow conformational exchange. One of these two centers of stacking interactions is highly conserved among the known HU and IHF proteins. Second aromatic core described recently in IHFs and IHF-like proteins is considered as a discriminating feature of IHFs. We performed an electromobility shift assay to confirm high affinities of HUSpm to both normal and distorted dsDNA, which are the characteristics of HU protein. MD simulations of HUSpm with alanine mutations of the residues forming the non-conserved aromatic cluster demonstrate its role in dimer stabilization, as both partial and complete distortion of the cluster enhances local flexibility of HUSpm.

Structural plasticity and thermal stability of the histone-like protein from Spiroplasma melliferum are due to phenylalanine insertions into the conservative scaffold.,Timofeev VI, Altukhov DA, Talyzina AA, Agapova YK, Vlaskina AV, Korzhenevskiy DA, Kleymenov SY, Bocharov EV, Rakitina TV J Biomol Struct Dyn. 2018 Dec;36(16):4392-4404. doi: , 10.1080/07391102.2017.1417162. Epub 2018 Jan 7. PMID:29283021<ref>PMID:29283021</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7pzo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dermatophagoides pteronyssinus]]
[[Category: Large Structures]]
[[Category: Abramchik YA]]
[[Category: Esipov RS]]
[[Category: Kostromina MA]]
[[Category: Kuranova IP]]
[[Category: Lykoshin DD]]
[[Category: Mikheeva OO]]
[[Category: Shevtsov MB]]
[[Category: Timofeev VI]]
[[Category: Zavriev SK]]
[[Category: Zayats EA]]