FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2298826212> ?p ?o ?g. }

• W2298826212 endingPage "1740" @default.
• W2298826212 startingPage "1724" @default.
• W2298826212 abstract "Plant hemoglobins constitute three distinct groups: symbiotic, nonsymbiotic, and truncated hemoglobins. Structural investigation of symbiotic and nonsymbiotic (class I) hemoglobins revealed the presence of a vertebrate-like 3/3 globin fold in these proteins. In contrast, plant truncated hemoglobins are similar to bacterial truncated hemoglobins with a putative 2/2 α-helical globin fold. While multiple structures have been reported for plant hemoglobins of the first two categories, for plant truncated globins only one structure has been reported of late. Here, we report yet another crystal structure of the truncated hemoglobin from Arabidopsis thaliana (AHb3) with two water molecules in the heme pocket, of which one is distinctly coordinated to the heme iron, unlike the only available crystal structure of AHb3 with a hydroxyl ligand. AHb3 was monomeric in its crystallographic asymmetric unit; however, dimer was evident in the crystallographic symmetry, and the globin indeed existed as a stable dimer in solution. The tertiary structure of the protein exhibited a bacterial-like 2/2 α-helical globin fold with an additional N-terminal α-helical extension and disordered C-termini. To address the role of these extended termini in AHb3, which is yet unknown, N- and C-terminal deletion mutants were created and characterized and molecular dynamics simulations performed. The C-terminal deletion had an insignificant effect on most properties but perturbed the dimeric equilibrium of AHb3 and significantly influenced azide binding kinetics in the ferric state. These results along with the disordered nature of the C-terminus indicated its putative role in intramolecular or intermolecular interactions probably regulating protein-ligand and protein-protein interactions. While the N-terminal deletion did not change the overall globin fold, stability, or ligand binding kinetics, it seemed to have influenced coordination at the heme iron, the hydration status of the active site, and the quaternary structure of AHb3. Evidence indicated that the N-terminus is the predominant factor regulating the quaternary interaction appropriate to physiological requirements, dynamics of the side chains in the heme pocket, and tunnel organization in the protein matrix." @default.
• W2298826212 created "2016-06-24" @default.
• W2298826212 creator A5022819280 @default.
• W2298826212 creator A5031944621 @default.
• W2298826212 creator A5052838748 @default.
• W2298826212 creator A5060702151 @default.
• W2298826212 creator A5070464641 @default.
• W2298826212 creator A5075373540 @default.
• W2298826212 creator A5076152057 @default.
• W2298826212 creator A5078189605 @default.
• W2298826212 date "2016-03-07" @default.
• W2298826212 modified "2023-09-24" @default.
• W2298826212 title "Structural and Functional Significance of the N- and C-Terminal Appendages in Arabidopsis Truncated Hemoglobin" @default.
• W2298826212 cites W113763381 @default.
• W2298826212 cites W1494809784 @default.
• W2298826212 cites W1506664007 @default.
• W2298826212 cites W1539796472 @default.
• W2298826212 cites W1963701924 @default.
• W2298826212 cites W1965668388 @default.
• W2298826212 cites W1966041739 @default.
• W2298826212 cites W1984698654 @default.
• W2298826212 cites W1984788157 @default.
• W2298826212 cites W1987134040 @default.
• W2298826212 cites W1987398418 @default.
• W2298826212 cites W1993957411 @default.
• W2298826212 cites W1994840640 @default.
• W2298826212 cites W1997993932 @default.
• W2298826212 cites W2001549223 @default.
• W2298826212 cites W2001641653 @default.
• W2298826212 cites W2001786349 @default.
• W2298826212 cites W2003558751 @default.
• W2298826212 cites W2004826935 @default.
• W2298826212 cites W2006773422 @default.
• W2298826212 cites W2010474135 @default.
• W2298826212 cites W2013745278 @default.
• W2298826212 cites W2017785367 @default.
• W2298826212 cites W2025527648 @default.
• W2298826212 cites W2025864461 @default.
• W2298826212 cites W2027091658 @default.
• W2298826212 cites W2028350877 @default.
• W2298826212 cites W2029389133 @default.
• W2298826212 cites W2029667189 @default.
• W2298826212 cites W2035503835 @default.
• W2298826212 cites W2042206208 @default.
• W2298826212 cites W2043059065 @default.
• W2298826212 cites W2043371017 @default.
• W2298826212 cites W2055045227 @default.
• W2298826212 cites W2061737406 @default.
• W2298826212 cites W2069879369 @default.
• W2298826212 cites W2073774277 @default.
• W2298826212 cites W2073920851 @default.
• W2298826212 cites W2077547350 @default.
• W2298826212 cites W2081299490 @default.
• W2298826212 cites W2087316109 @default.
• W2298826212 cites W2091108104 @default.
• W2298826212 cites W2094342495 @default.
• W2298826212 cites W2098406639 @default.
• W2298826212 cites W2103846710 @default.
• W2298826212 cites W2104666616 @default.
• W2298826212 cites W2112880344 @default.
• W2298826212 cites W2116536808 @default.
• W2298826212 cites W2119547158 @default.
• W2298826212 cites W2120197945 @default.
• W2298826212 cites W2122150311 @default.
• W2298826212 cites W2125637986 @default.
• W2298826212 cites W2132262459 @default.
• W2298826212 cites W2133157119 @default.
• W2298826212 cites W2138747916 @default.
• W2298826212 cites W2140387095 @default.
• W2298826212 cites W2141872725 @default.
• W2298826212 cites W2142031796 @default.
• W2298826212 cites W2144081223 @default.
• W2298826212 cites W2150981663 @default.
• W2298826212 cites W2154725664 @default.
• W2298826212 cites W2154920112 @default.
• W2298826212 cites W2156341767 @default.
• W2298826212 cites W2158076215 @default.
• W2298826212 cites W2158763240 @default.
• W2298826212 cites W2159211495 @default.
• W2298826212 cites W2162101639 @default.
• W2298826212 cites W2165581033 @default.
• W2298826212 cites W2166805374 @default.
• W2298826212 cites W2313163796 @default.
• W2298826212 cites W4231956143 @default.
• W2298826212 cites W4241352628 @default.
• W2298826212 cites W957564342 @default.
• W2298826212 doi "https://doi.org/10.1021/acs.biochem.5b01013" @default.
• W2298826212 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26913482" @default.
• W2298826212 hasPublicationYear "2016" @default.
• W2298826212 type Work @default.
• W2298826212 sameAs 2298826212 @default.
• W2298826212 citedByCount "7" @default.
• W2298826212 countsByYear W22988262122017 @default.
• W2298826212 countsByYear W22988262122018 @default.
• W2298826212 countsByYear W22988262122020 @default.
• W2298826212 crossrefType "journal-article" @default.
• W2298826212 hasAuthorship W2298826212A5022819280 @default.
• W2298826212 hasAuthorship W2298826212A5031944621 @default.

• next