6hdd: Difference between revisions

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'''Unreleased structure'''


The entry 6hdd is ON HOLD  until Paper Publication
==OBP chaperonin in the nucleotide-free state==
<SX load='6hdd' size='340' side='right' viewer='molstar' caption='[[6hdd]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6hdd]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens_bacteriophage_obp Pseudomonas fluorescens bacteriophage obp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HDD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6HDD FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OBP_246 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1124849 Pseudomonas fluorescens bacteriophage OBP])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6hdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hdd OCA], [http://pdbe.org/6hdd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hdd RCSB], [http://www.ebi.ac.uk/pdbsum/6hdd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hdd ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Chaperonins are ubiquitously present protein complexes, which assist the proper folding of newly synthesized proteins and prevent aggregation of denatured proteins in an ATP-dependent manner. They are classified into group I (bacterial, mitochondrial, chloroplast chaperonins) and group II (archaeal and eukaryotic cytosolic variants). However, both of these groups do not include recently discovered viral chaperonins. Here, we solved the symmetry-free cryo-EM structures of a single-ring chaperonin encoded by the gene 246 of bacteriophage OBP Pseudomonas fluorescens, in the nucleotide-free, ATPgammaS-, and ADP-bound states, with a resolution of 4.3A, 5.0A, and 6A, respectively. The structure of OBP chaperonin reveals a unique subunit arrangement, with three subunits pairs and one unpaired subunit. Each pair combines subunits in two possible conformations, differing in nucleotide-binding affinity. Binding of nucleotides result in the increase of subunits' conformational variability. Due to its unique structural and functional features, OBP chaperonin can represent a new group. 148 words.


Authors: Semenyuk, P.I., Stanishneva-Konovalova, T.B., Sokolova, O.S.
Cryo-EM reveals an asymmetry in a novel single-ring viral chaperonin.,Stanishneva-Konovalova TB, Semenyuk PI, Kurochkina LP, Pichkur EB, Vasilyev AL, Kovalchuk MV, Kirpichnikov MP, Sokolova OS J Struct Biol. 2019 Dec 20:107439. doi: 10.1016/j.jsb.2019.107439. PMID:31870903<ref>PMID:31870903</ref>


Description: OBP chaperonin in the nucleotide-free state
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Semenyuk, P.I]]
<div class="pdbe-citations 6hdd" style="background-color:#fffaf0;"></div>
[[Category: Stanishneva-Konovalova, T.B]]
== References ==
[[Category: Sokolova, O.S]]
<references/>
__TOC__
</SX>
[[Category: Large Structures]]
[[Category: Pseudomonas fluorescens bacteriophage obp]]
[[Category: Semenyuk, P I]]
[[Category: Sokolova, O S]]
[[Category: Stanishneva-Konovalova, T B]]
[[Category: Chaperone]]
[[Category: Chaperonin]]
[[Category: Nucleotide-free]]
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