MBOAT
Identifiers
SymbolMBOAT
PfamPF03062
Pfam clanCL0517
InterProIPR004299
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
MBOAT_2
Identifiers
SymbolMBOAT_2
PfamPF13813
Pfam clanCL0517
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The MBOAT (membrane bound O-acyl transferase) family of membrane proteins is a family of various acyltransferase enzymes. All family members contain multiple transmembrane domains and most carry two conserved residues, a conserved histidine (His) embedded in a hydrophobic stretch of residues and an asparagine (Asn) or histidine within a more hydrophilic region some 30-50 residues upstream.[1]

MBOAT enzymes catalyze the transfer of an acyl group from an acyl-coenzyme or accessory protein to one of several different substrates. The family is found from bacteria to eukaryotes.[2]

The family may be grouped into three categories, according to function:

  1. enzymes involved in neutral lipid biosynthesis;
  2. enzymes involved in protein/peptide acylation;
  3. enzymes involved in phospholipid re-modelling.[3]

Structure

The structure for one MBOAT protein, DltB from Streptococcus thermophilus (Q5M4V4), has been solved. DltB performs D-alanylation of cell-wall teichoic acid. It contains a ring of 11 transmembrane helices surrounding a tunnel that goes through the biological membrane. The tunnel connects to a partner, DltC, which carries the D-alanine to the conserved histidine residue of DltB MBOAT located at the bottom of the funnel.[4] A computational model of human ghrelin O-acyltransferase (GOAT) (Q96T53) revealed a transmembrane channel that facilitates octanoylation of the peptide hormone ghrelin.[5] DltB and GOAT share structural similarities in their homologous regions, suggesting a common core fold for MBOAT family members.

Human proteins with this domain

References

  1. ↑ Hofmann K (March 2000). "A superfamily of membrane-bound O-acyltransferases with implications for wnt signaling". Trends Biochem. Sci. 25 (3): 111–2. doi:10.1016/s0968-0004(99)01539-x. PMID 10694878.
  2. ↑ Chang, C.C.Y., Sun, J. & Chang, TY. (2011). "Membrane-bound O-acyltransferases (MBOATs)". Front. Biol. 6 (3): 177. doi:10.1007/s11515-011-1149-z. S2CID 41626991.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  3. ↑ Wang P, Wang Z, Dou Y, Zhang X, Wang M, Tian X (2013). "Genome-wide identification and analysis of membrane-bound O-acyltransferase (MBOAT) gene family in plants". Planta. 238 (5): 907–22. Bibcode:2013Plant.238..907W. doi:10.1007/s00425-013-1939-4. PMID 23928653. S2CID 1328304.
  4. ↑ Ma, D; Wang, Z; Merrikh, CN; Lang, KS; Lu, P; Li, X; Merrikh, H; Rao, Z; Xu, W (October 2018). "Crystal structure of a membrane-bound O-acyltransferase". Nature. 562 (7726): 286–290. Bibcode:2018Natur.562..286M. doi:10.1038/s41586-018-0568-2. PMC 6529733. PMID 30283133.
  5. ↑ Campaña, Maria B.; Irudayanathan, Flaviyan Jerome; Davis, Tasha R.; McGovern-Gooch, Kayleigh R.; Loftus, Rosemary; Ashkar, Mohammad; Escoffery, Najae; Navarro, Melissa; Sieburg, Michelle A.; Nangia, Shikha; Hougland, James L. (27 September 2019). "The ghrelin O-acyltransferase structure reveals a catalytic channel for transmembrane hormone acylation". The Journal of Biological Chemistry. 294 (39): 14166–14174. doi:10.1074/jbc.AC119.009749. ISSN 1083-351X. PMC 6768652. PMID 31413115.
    This article incorporates text from the public domain Pfam and InterPro: IPR004299
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