4QSG: Crystal Structure Of Gas Vesicle Protein Gvpf From Microcystis Aeruginosa

Citation:
Abstract
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.
PDB ID: 4QSGDownload
MMDB ID: 124678
PDB Deposition Date: 2014/7/3
Updated in MMDB: 2014/11
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 4QSG: monomeric; determined by author and by software (PISA)
Molecular Components in 4QSG
Label Count Molecule
Protein (1 molecule)
1
GAS Vesicle Protein
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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