1umo: Difference between revisions
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[[Image:1umo.gif|left|200px]]<br /><applet load="1umo" size=" | [[Image:1umo.gif|left|200px]]<br /><applet load="1umo" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1umo, resolution 2.59Å" /> | caption="1umo, resolution 2.59Å" /> | ||
'''THE CRYSTAL STRUCTURE OF CYTOGLOBIN: THE FOURTH GLOBIN TYPE DISCOVERED IN AMN'''<br /> | '''THE CRYSTAL STRUCTURE OF CYTOGLOBIN: THE FOURTH GLOBIN TYPE DISCOVERED IN AMN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1UMO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Hem Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | 1UMO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Hem+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMO OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transport]] | [[Category: transport]] | ||
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Revision as of 11:02, 3 February 2008
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THE CRYSTAL STRUCTURE OF CYTOGLOBIN: THE FOURTH GLOBIN TYPE DISCOVERED IN AMN
OverviewOverview
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 StructureAbout this Structure
1UMO is a Single protein structure of sequence from Homo sapiens with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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
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