6svf | pdb_00006svf

Crystal structure of the P235GK mutant of ArgBP from T. maritima

spinqualitylabelsall models 6svf, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6svf is a 1 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: ARG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9WZ62_THEMA Publication Abstract from PubMed Domain swapping is a widespread oligomerization process that is observed in a large variety of protein families. In the large superfamily of substrate-binding proteins, non-monomeric members have rarely been reported. The arginine-binding protein from Thermotoga maritima (TmArgBP), a protein endowed with a number of unusual properties, presents a domain-swapped structure in its dimeric native state in which the two polypeptide chains mutually exchange their C-terminal helices. It has previously been shown that mutations in the region connecting the last two helices of the TmArgBP structure lead to the formation of a variety of oligomeric states (monomers, dimers, trimers and larger aggregates). With the aim of defining the structural determinants of domain swapping in TmArgBP, the monomeric form of the P235GK mutant has been structurally characterized. Analysis of this arginine-bound structure indicates that it consists of a closed monomer with its C-terminal helix folded against the rest of the protein, as typically observed for substrate-binding proteins. Notably, the two terminal helices are joined by a single nonhelical residue (Gly235). Collectively, the present findings indicate that extending the hinge region and conferring it with more conformational freedom makes the formation of a closed TmArgBP monomer possible. On the other hand, the short connection between the helices may explain the tendency of the protein to also adopt alternative oligomeric states (dimers, trimers and larger aggregates). The data reported here highlight the importance of evolutionary control to avoid the uncontrolled formation of heterogeneous and potentially harmful oligomeric species through domain swapping. The non-swapped monomeric structure of the arginine-binding protein from Thermotoga maritima.,Smaldone G, Ruggiero A, Balasco N, Abuhammad A, Autiero I, Caruso D, Esposito D, Ferraro G, Gelardi ELM, Moreira M, Quareshy M, Romano M, Saaret A, Selvam I, Squeglia F, Troisi R, Kroon-Batenburg LMJ, Esposito L, Berisio R, Vitagliano L Acta Crystallogr F Struct Biol Commun. 2019 Nov 1;75(Pt 11):707-713. doi:, 10.1107/S2053230X1901464X. Epub 2019 Nov 5. PMID:31702584 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ABC transporter 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA