Premium
The Uteroglobin Fold
Author(s) -
CALLEBAUT ISABELLE,
POUPON ANNE,
BALLY RÉNÉE,
DEMARET JEANPHILIPPE,
HOUSSET DOMINIQUE,
DELETTRÉ JEAN,
HOSSENLOPP PAUL,
MOR JEANPAUL
Publication year - 2000
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2000.tb05522.x
Subject(s) - uteroglobin , chemistry , hydrolase , monomer , crystallography , stereochemistry , biochemistry , biophysics , enzyme , biology , organic chemistry , gene , polymer
A bstract : Uteroglobin (UTG) forms a fascinating homodimeric structure that binds small‐ to medium‐sized ligands through an internal hydrophobic cavity, located at the interface between the two monomers. Previous studies have shown that UTG fold is not limited to the UTG/CC10 family, whose sequence/structure relationships are highlighted here, but can be extended to the cap domain of Xanthobacter autotrophicus haloalkane dehalogenase. We show here that UTG fold is adopted by several other cap domains within the α/β hydrolase family, making it a well‐suited “geode” structure allowing it to sequester various hydrophobic molecules. Additionally, some data about a new crystal form of oxidized rabbit UTG are presented, completing previous structural studies, as well as results from molecular dynamics, suggesting an alternative way for the ligand to reach the internal cavity.