The uteroglobin fold.
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 alpha/beta 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.
Callebaut
I
I
Systèmes Moléculaires et Biologie Structurale, Laboratoire de Minéralogie-Cristallographie Paris (LMCP), CNRS UMR 7590, Universités Paris 6 et Paris 7, Case 115, 4 Place Jussieu, 75252 Paris, France. Isabelle.Callebaut@lmcp.jussieu.fr
Poupon
A
A
Bally
R
R
Demaret
J P
JP
Housset
D
D
Delettré
J
J
Hossenlopp
P
P
Mornon
J P
JP
D000595:Amino Acid Sequence / Q000502:physiology; D000818:Animals; D016000:Cluster Analysis; D006801:Humans; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary / Q000502:physiology*; D014598:Uteroglobin / Q000737:chemistry*
D014598:Uteroglobin