1ux9
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MAPPING PROTEIN MATRIX CAVITIES IN HUMAN CYTOGLOBIN THROUGH XE ATOM BINDING: A CRYSTALLOGRAPHIC INVESTIGATION
OverviewOverview
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.
About this StructureAbout this Structure
1UX9 is a Single protein structure of sequence from Homo sapiens with XE, HEM and FC6 as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Mapping protein matrix cavities in human cytoglobin through Xe atom binding., de Sanctis D, Dewilde S, Pesce A, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M, Biochem Biophys Res Commun. 2004 Apr 16;316(4):1217-21. PMID:15044115
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