1ux9
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1ux9 |SIZE=350|CAPTION= <scene name='initialview01'>1ux9</scene>, resolution 2.4Å | |PDB= 1ux9 |SIZE=350|CAPTION= <scene name='initialview01'>1ux9</scene>, resolution 2.4Å | ||
|SITE= <scene name='pdbsite=AC1:Fc6+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Fc6+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=XE:XENON'>XE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ux9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ux9 OCA], [http://www.ebi.ac.uk/pdbsum/1ux9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ux9 RCSB]</span> | ||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: Pesce, A.]] | [[Category: Pesce, A.]] | ||
[[Category: Sanctis, D De.]] | [[Category: Sanctis, D De.]] | ||
| - | [[Category: FC6]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: XE]] | ||
[[Category: heme]] | [[Category: heme]] | ||
[[Category: oxygen storage/transport]] | [[Category: oxygen storage/transport]] | ||
[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:16:37 2008'' |
Revision as of 21:16, 30 March 2008
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MAPPING PROTEIN MATRIX CAVITIES IN HUMAN CYTOGLOBIN THROUGH XE ATOM BINDING: A CRYSTALLOGRAPHIC INVESTIGATION
Overview
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 Structure
1UX9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Mar 31 00:16:37 2008
