Matches in SemOpenAlex for { <https://semopenalex.org/work/W2738283313> ?p ?o ?g. }
- W2738283313 abstract "The monovalent anions formate, nitrite and hydrosulphide are main metabolites of bacterial respiration during anaerobic mixed-acid fermentation. When accumulated in the cytoplasm, these anions become cytotoxic. Membrane proteins that selectively transport these monovalent anions across the membrane have been identified and they belong to the family of Formate/Nitrite Transporters (FNTs). Individual members that selectively transport formate, nitrite and hydrosulphide have been investigated. Experimentally determined structures of FNTs indicate that they share the same hourglass helical fold with aquaporins and aquaglyceroporins and have two constriction regions, namely, cytoplasmic slit and central constriction. Members of FNTs are found in bacteria, archaea, fungi and protists. However, no FNT homolog has been identified in mammals. With FNTs as potential drug targets for many bacterial diseases, it is important to understand the mechanism of selectivity and transport across these transporters.We have systematically searched the sequence databases and identified 2206 FNT sequences from bacteria, archaea and eukaryotes. Although FNT sequences are very diverse, homology modeling followed by structure-based sequence alignment revealed that nearly one third of all the positions within the transmembrane region exhibit high conservation either as a group or at the level of individual residues across all three kingdoms. Phylogenetic analysis of prokaryotic FNT sequences revealed eight different subgroups. Formate, nitrite and hydrosulphide transporters respectively are clustered into two (FocA and FdhC), three (NirC-α, NirC-β and NirC-γ) and one (HSC) subfamilies. We have also recognized two FNT subgroups (YfdC-α and YfdC-β) with unassigned function. Analysis of taxonomic distribution indicates that each subfamily prefers specific taxonomic groups. Structure-based sequence alignment of individual subfamily members revealed that certain positions in the two constriction regions and some residues facing the interior show subfamily-specific conservation. We have also identified examples of FNTs with the two constriction regions formed by residues that are less frequently observed. We have developed dbFNT, a database of FNT models and associated details. dbFNT is freely available to scientific community.Taxonomic distribution and sequence conservation of FNTs exhibit subfamily-specific features. The conservation pattern in the central constriction and cytoplasmic slit in the open and closed states are distinct for YfdC and NirC subfamilies. The same is true for some residues facing the interior of the transporters. The specific residues in these positions can exert influence on the type of solutes that are transported by these proteins. With FNTs found in many disease-causing bacteria, the knowledge gained in this study can be used in the development and design of anti-bacterial drugs." @default.
- W2738283313 created "2017-07-31" @default.
- W2738283313 creator A5006591304 @default.
- W2738283313 creator A5052888865 @default.
- W2738283313 creator A5066718312 @default.
- W2738283313 date "2017-07-24" @default.
- W2738283313 modified "2023-10-18" @default.
- W2738283313 title "Anion-selective Formate/nitrite transporters: taxonomic distribution, phylogenetic analysis and subfamily-specific conservation pattern in prokaryotes" @default.
- W2738283313 cites W1528475631 @default.
- W2738283313 cites W1539843091 @default.
- W2738283313 cites W1555301616 @default.
- W2738283313 cites W1607931568 @default.
- W2738283313 cites W1925420621 @default.
- W2738283313 cites W1963621312 @default.
- W2738283313 cites W1968364488 @default.
- W2738283313 cites W1971147414 @default.
- W2738283313 cites W1975304761 @default.
- W2738283313 cites W1986191025 @default.
- W2738283313 cites W1993152899 @default.
- W2738283313 cites W1999531492 @default.
- W2738283313 cites W2001017384 @default.
- W2738283313 cites W2001573278 @default.
- W2738283313 cites W2002360764 @default.
- W2738283313 cites W2009530683 @default.
- W2738283313 cites W2015403140 @default.
- W2738283313 cites W2018620177 @default.
- W2738283313 cites W2024260356 @default.
- W2738283313 cites W2029667189 @default.
- W2738283313 cites W2033503608 @default.
- W2738283313 cites W2035816104 @default.
- W2738283313 cites W2048743237 @default.
- W2738283313 cites W2058658881 @default.
- W2738283313 cites W2062018285 @default.
- W2738283313 cites W2064997088 @default.
- W2738283313 cites W2065283382 @default.
- W2738283313 cites W2068362408 @default.
- W2738283313 cites W2069771830 @default.
- W2738283313 cites W2075355025 @default.
- W2738283313 cites W2078936885 @default.
- W2738283313 cites W2079916438 @default.
- W2738283313 cites W2084304818 @default.
- W2738283313 cites W2088311074 @default.
- W2738283313 cites W2092398899 @default.
- W2738283313 cites W2093602334 @default.
- W2738283313 cites W2097870001 @default.
- W2738283313 cites W2105546584 @default.
- W2738283313 cites W2107158607 @default.
- W2738283313 cites W2108152992 @default.
- W2738283313 cites W2114347076 @default.
- W2738283313 cites W2114489396 @default.
- W2738283313 cites W2116520673 @default.
- W2738283313 cites W2126943884 @default.
- W2738283313 cites W2127868864 @default.
- W2738283313 cites W2134603596 @default.
- W2738283313 cites W2135719986 @default.
- W2738283313 cites W2137037625 @default.
- W2738283313 cites W2141052558 @default.
- W2738283313 cites W2141563676 @default.
- W2738283313 cites W2148534890 @default.
- W2738283313 cites W2148698435 @default.
- W2738283313 cites W2149104046 @default.
- W2738283313 cites W2152770371 @default.
- W2738283313 cites W2153911335 @default.
- W2738283313 cites W2156125289 @default.
- W2738283313 cites W2158714788 @default.
- W2738283313 cites W2160544821 @default.
- W2738283313 cites W2160867136 @default.
- W2738283313 cites W2164461702 @default.
- W2738283313 cites W2164954842 @default.
- W2738283313 cites W2170747616 @default.
- W2738283313 cites W2183813763 @default.
- W2738283313 cites W2224056471 @default.
- W2738283313 cites W2282669519 @default.
- W2738283313 cites W2336330109 @default.
- W2738283313 cites W2593775203 @default.
- W2738283313 cites W2605068739 @default.
- W2738283313 cites W2739999456 @default.
- W2738283313 cites W3206572385 @default.
- W2738283313 cites W4211140781 @default.
- W2738283313 cites W4211156111 @default.
- W2738283313 cites W4254455346 @default.
- W2738283313 doi "https://doi.org/10.1186/s12864-017-3947-4" @default.
- W2738283313 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5525234" @default.
- W2738283313 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28738779" @default.
- W2738283313 hasPublicationYear "2017" @default.
- W2738283313 type Work @default.
- W2738283313 sameAs 2738283313 @default.
- W2738283313 citedByCount "18" @default.
- W2738283313 countsByYear W27382833132018 @default.
- W2738283313 countsByYear W27382833132019 @default.
- W2738283313 countsByYear W27382833132020 @default.
- W2738283313 countsByYear W27382833132022 @default.
- W2738283313 countsByYear W27382833132023 @default.
- W2738283313 crossrefType "journal-article" @default.
- W2738283313 hasAuthorship W2738283313A5006591304 @default.
- W2738283313 hasAuthorship W2738283313A5052888865 @default.
- W2738283313 hasAuthorship W2738283313A5066718312 @default.
- W2738283313 hasBestOaLocation W27382833131 @default.
- W2738283313 hasConcept C104317684 @default.
- W2738283313 hasConcept C149011108 @default.