1ut0

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[[Image:1ut0.jpg|left|200px]]
[[Image:1ut0.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1ut0 |SIZE=350|CAPTION= <scene name='initialview01'>1ut0</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1ut0", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Fc6+Binding+Site+For+Chain+B'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1ut0| PDB=1ut0 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ut0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ut0 OCA], [http://www.ebi.ac.uk/pdbsum/1ut0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ut0 RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF CYTOGLOBIN: THE FOURTH GLOBIN TYPE DISCOVERED IN MAN DISPLAYS HEME HEXA-COORDINATION'''
'''CRYSTAL STRUCTURE OF CYTOGLOBIN: THE FOURTH GLOBIN TYPE DISCOVERED IN MAN DISPLAYS HEME HEXA-COORDINATION'''
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[[Category: Pesce, A.]]
[[Category: Pesce, A.]]
[[Category: Sanctis, D De.]]
[[Category: Sanctis, D De.]]
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[[Category: cytoglobin]]
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[[Category: Cytoglobin]]
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[[Category: heme]]
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[[Category: Heme]]
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[[Category: hemoglobin]]
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[[Category: Hemoglobin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:38:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:14:48 2008''
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Revision as of 08:38, 3 May 2008

Image:1ut0.jpg

Template:STRUCTURE 1ut0

CRYSTAL STRUCTURE OF CYTOGLOBIN: THE FOURTH GLOBIN TYPE DISCOVERED IN MAN DISPLAYS HEME HEXA-COORDINATION


Overview

Cytoglobin is a recently discovered hemeprotein belonging to the globin superfamily together with hemoglobin, myoglobin and neuroglobin. Although distributed in almost all human tissues, cytoglobin has not been ascribed a specific function. Human cytoglobin is composed of 190 amino acid residues. Sequence alignments show that a protein core region (about 150 residues) is structurally related to hemoglobin and myoglobin, being complemented by about 20 extra residues both on the N and C termini. In the absence of exogenous ligands (e.g. O2), the cytoglobin distal HisE7 residue is coordinated to the heme Fe atom, thus decreasing the ligand affinity. The crystal structure of human cytoglobin (2.1 A resolution, 21.3% R-factor) highlights a three-over-three alpha-helical globin fold, covering residues 18-171; the 1-17 N-terminal, and the 172-190 C-terminal residue segments are disordered in both molecules of the crystal asymmetric unit. Heme hexa-coordination is evident in one of the two cytoglobin chains, whereas alternate conformation for the heme distal region, achieving partial heme penta-coordination, is observed in the other. Human cytoglobin displays a large apolar protein matrix cavity, next to the heme, not related to the myoglobin cavities recognized as temporary ligand docking stations. The cavity, which may provide a heme ligand diffusion pathway, is connected to the external space through a narrow tunnel nestled between the globin G and H helices.

About this Structure

1UT0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of cytoglobin: the fourth globin type discovered in man displays heme hexa-coordination., de Sanctis D, Dewilde S, Pesce A, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M, J Mol Biol. 2004 Feb 27;336(4):917-27. PMID:15095869 Page seeded by OCA on Sat May 3 11:38:49 2008

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