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1UX9

Mapping protein matrix cavities in human cytoglobin through Xe atom binding: a crystallographic investigation

Summary for 1UX9
Entry DOI10.2210/pdb1ux9/pdb
Related1UMO 1URV 1URY 1UT0
DescriptorCYTOGLOBIN, XENON, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
Functional Keywordsoxygen transport, oxygen storage/transport, heme, transport
Biological sourceHOMO SAPIENS
Cellular locationCytoplasm (By similarity): Q8WWM9
Total number of polymer chains2
Total formula weight45378.89
Authors
De Sanctis, D.,Dewilde, S.,Pesce, A.,Moens, L.,Ascenzi, P.,Hankeln, T.,Burmester, T.,Bolognesi, M. (deposition date: 2004-02-23, release date: 2004-06-01, Last modification date: 2024-05-08)
Primary citationDe Sanctis, D.,Dewilde, S.,Pesce, A.,Moens, L.,Ascenzi, P.,Hankeln, T.,Burmester, T.,Bolognesi, M.
Mapping Protein Matrix Cavities in Human Cytoglobin Through Xe Atom Binding
Biochem.Biophys.Res.Commun., 316:1217-, 2004
Cited by
PubMed 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.
PubMed: 15044115
DOI: 10.1016/J.BBRC.2004.03.007
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

226707

數據於2024-10-30公開中

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