4qsg

</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=4qsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qsg OCA], [https://pdbe.org/4qsg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qsg RCSB], [https://www.ebi.ac.uk/pdbsum/4qsg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qsg ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Gas vesicles are gas-filled proteinaceous organelles that provide buoyancy for bacteria and archaea. A gene cluster that is highly conserved in various species encodes about 8-14 proteins (Gvp proteins) that are involved in the formation of gas vesicles. Here, the first crystal structure of the gas vesicle protein GvpF from Microcystis aeruginosa PCC 7806 is reported at 2.7 A resolution. GvpF is composed of two structurally distinct domains (the N-domain and C-domain), both of which display an alpha+beta class overall structure. The N-domain adopts a novel fold, whereas the C-domain has a modified ferredoxin fold with an apparent variation owing to an extension region consisting of three sequential helices. The two domains pack against each other via interactions with a C-terminal tail that is conserved among cyanobacteria. Taken together, it is concluded that the overall architecture of GvpF presents a novel fold. Moreover, it is shown that GvpF is most likely to be a structural protein that is localized at the gas-facing surface of the gas vesicle by immunoblotting and immunogold labelling-based tomography.

Structure of the gas vesicle protein GvpF from the cyanobacterium Microcystis aeruginosa.,Xu BY, Dai YN, Zhou K, Liu YT, Sun Q, Ren YM, Chen Y, Zhou CZ Acta Crystallogr D Biol Crystallogr. 2014 Nov;70(Pt 11):3013-22. doi:, 10.1107/S1399004714021312. Epub 2014 Oct 29. PMID:25372690<ref>PMID:25372690</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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