Open AccessStructure of the first representative of Pfam family PF09410 (DUF2006) reveals a structural signature of the calycin superfamily that suggests a role in lipid metabolism
Author(s) -
Chiu HsiuJu,
Bakolitsa Constantina,
Skerra Arne,
Lomize Andrei,
Carlton Dennis,
Miller Mitchell D.,
Krishna S. Sri,
Abdubek Polat,
Astakhova Tamara,
Axelrod Herbert L.,
Clayton Thomas,
Deller Marc C.,
Duan Lian,
Feuerhelm Julie,
Grant Joanna C.,
Grzechnik Slawomir K.,
Han Gye Won,
Jaroszewski Lukasz,
Jin Kevin K.,
Klock Heath E.,
Knuth Mark W.,
Kozbial Piotr,
Kumar Abhinav,
Marciano David,
McMullan Daniel,
Morse Andrew T.,
Nigoghossian Edward,
Okach Linda,
Paulsen Jessica,
Reyes Ron,
Rife Christopher L.,
Van Den Bedem Henry,
Weekes Dana,
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/s1744309109037749
Subject(s) - structural similarity , biology , lipocalin , computational biology , function (biology) , protein family , domain (mathematical analysis) , lipid metabolism , gene duplication , sequence alignment , sequence (biology) , biochemistry , genetics , peptide sequence , gene , mathematical analysis , mathematics
The first structural representative of the domain of unknown function DUF2006 family, also known as Pfam family PF09410, comprises a lipocalin‐like fold with domain duplication. The finding of the calycin signature in the N‐terminal domain, combined with remote sequence similarity to two other protein families (PF07143 and PF08622) implicated in isoprenoid metabolism and the oxidative stress response, support an involvement in lipid metabolism. Clusters of conserved residues that interact with ligand mimetics suggest that the binding and regulation sites map to the N‐terminal domain and to the interdomain interface, respectively.