 |
PDBsum entry 1ux9
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Oxygen transport
|
PDB id
|
|
|
|
1ux9
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Mapping protein matrix cavities in human cytoglobin through xe atom binding.
|
|
|
Authors
|
|
D.De sanctis,
S.Dewilde,
A.Pesce,
L.Moens,
P.Ascenzi,
T.Hankeln,
T.Burmester,
M.Bolognesi.
|
|
|
Ref.
|
|
Biochem Biophys Res Commun, 2004,
316,
1217-1221.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Cytoglobin is the fourth recognized globin type, almost ubiquitously distributed
in human tissues; its function is still poorly understood. Cytoglobin displays a
core region of about 150 residues, structurally related to hemoglobin and
myoglobin, and two extra segments, about 20 residues each, at the N- and
C-termini. The core region hosts a large apolar cavity, held to provide a ligand
diffusion pathway to/from the heme, and/or ligand temporary docking sites. Here
we report the crystal structure (2.4A resolution, R-factor 19.1%) of a human
cytoglobin mutant bearing the CysB2(38) --> Ser and CysE9(83) --> Ser
substitutions (CYGB*), treated under pressurized xenon. Three Xe atoms bind to
the heme distal site region of CYGB* mapping the protein matrix apolar cavity.
Despite the conserved globin fold, the cavity found in CYGB* is structured
differently from those recognized to play a functional role in myoglobin,
neuroglobin, truncated hemoglobins, and Cerebratulus lacteus mini-hemoglobin.
|
|
|
|
|
|
|
