Open AccessThe structure of the first representative of Pfam family PF06475 reveals a new fold with possible involvement in glycolipid metabolism
Author(s) -
Bakolitsa Constantina,
Kumar Abhinav,
McMullan Daniel,
Krishna S. Sri,
Miller Mitchell D.,
Carlton Dennis,
Najmanovich Rafael,
Abdubek Polat,
Astakhova Tamara,
Chiu HsiuJu,
Clayton Thomas,
Deller Marc C.,
Duan Lian,
Elias Ylva,
Feuerhelm Julie,
Grant Joanna C.,
Grzechnik Slawomir K.,
Han Gye Won,
Jaroszewski Lukasz,
Jin Kevin K.,
Klock Heath E.,
Knuth Mark W.,
Kozbial Piotr,
Marciano David,
Morse Andrew T.,
Nigoghossian Edward,
Okach Linda,
Oommachen Silvya,
Paulsen Jessica,
Reyes Ron,
Rife Christopher L.,
Trout Christina V.,
Van Den Bedem Henry,
Weekes Dana,
White Aprilfawn,
Xu Qingping,
Hodgson Keith O.,
Wooley John,
Elsliger MarcAndré,
Deacon Ashley M.,
Godzik Adam,
Lesley Scott A.,
Wilson Ian A.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109022684
Subject(s) - glycolipid , context (archaeology) , biochemistry , lipid metabolism , protein family , biology , metabolism , chemistry , gene , paleontology
The crystal structure of PA1994 from Pseudomonas aeruginosa , a member of the Pfam PF06475 family classified as a domain of unknown function (DUF1089), reveals a novel fold comprising a 15‐stranded β‐sheet wrapped around a single α‐helix that assembles into a tight dimeric arrangement. The remote structural similarity to lipoprotein localization factors, in addition to the presence of an acidic pocket that is conserved in DUF1089 homologs, phospholipid‐binding and sugar‐binding proteins, indicate a role for PA1994 and the DUF1089 family in glycolipid metabolism. Genome‐context analysis lends further support to the involvement of this family of proteins in glycolipid metabolism and indicates possible activation of DUF1089 homologs under conditions of bacterial cell‐wall stress or host–pathogen interactions.