View source for 2ndp


==Structure of DNA-binding HU protein from micoplasma Mycoplasma gallisepticum==
<StructureSection load='2ndp' size='340' side='right'caption='[[2ndp]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ndp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycoplasma_gallisepticum_S6 Mycoplasma gallisepticum S6]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NDP FirstGlance]. <br>
</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=2ndp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ndp OCA], [https://pdbe.org/2ndp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ndp RCSB], [https://www.ebi.ac.uk/pdbsum/2ndp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ndp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0F6CKR5_MYCGL A0A0F6CKR5_MYCGL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The histone-like (HU) protein is one of the major nucleoid-associated proteins involved in DNA supercoiling and compaction into bacterial nucleoid as well as in all DNA-dependent transactions. This small positively charged dimeric protein binds DNA in a non-sequence specific manner promoting DNA super-structures. The majority of HU proteins are highly conserved among bacteria; however, HU protein from Mycoplasma gallisepticum (HUMgal) has multiple amino acid substitutions in the most conserved regions, which are believed to contribute to its specificity to DNA targets unusual for canonical HU proteins. In this work, we studied the structural dynamic properties of the HUMgal dimer by NMR spectroscopy and MD simulations. The obtained all-atom model displays compliance with the NMR data and confirms the heterogeneous backbone flexibility of HUMgal. We found that HUMgal, being folded into a dimeric conformation typical for HU proteins, has a labile alpha-helical body with protruded beta-stranded arms forming DNA-binding domain that are highly flexible in the absence of DNA. The amino acid substitutions in conserved regions of the protein are likely to affect the conformational lability of the HUMgal dimer that can be responsible for complex functional behavior of HUMgal in vivo, e.g. facilitating its spatial adaptation to non-canonical DNA-targets.

Enhanced conformational flexibility of the histone-like (HU) protein from Mycoplasma gallisepticum.,Altukhov DA, Talyzina AA, Agapova YK, Vlaskina AV, Korzhenevskiy DA, Bocharov EV, Rakitina TV, Timofeev VI, Popov VO J Biomol Struct Dyn. 2018 Jan;36(1):45-53. doi: 10.1080/07391102.2016.1264893., Epub 2016 Dec 29. PMID:27884082<ref>PMID:27884082</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ndp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycoplasma gallisepticum S6]]
[[Category: Agapova YK]]
[[Category: Altukhov DA]]
[[Category: Bocharov EV]]
[[Category: Korzhenevskiy DA]]
[[Category: Popov VO]]
[[Category: Rakitina TV]]
[[Category: Talyzina AA]]
[[Category: Timofeev VI]]
[[Category: Vlaskina AV]]