1bcf
From Proteopedia
(New page: 200px<br /><applet load="1bcf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bcf, resolution 2.9Å" /> '''THE STRUCTURE OF A UN...) |
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| - | [[Image:1bcf.gif|left|200px]]<br /><applet load="1bcf" size=" | + | [[Image:1bcf.gif|left|200px]]<br /><applet load="1bcf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bcf, resolution 2.9Å" /> | caption="1bcf, resolution 2.9Å" /> | ||
'''THE STRUCTURE OF A UNIQUE, TWO-FOLD SYMMETRIC, HAEM-BINDING SITE'''<br /> | '''THE STRUCTURE OF A UNIQUE, TWO-FOLD SYMMETRIC, HAEM-BINDING SITE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacterioferritin of Escherichia coli, also known as cytochrome b1, is a | + | Bacterioferritin of Escherichia coli, also known as cytochrome b1, is a hollow, nearly spherical shell made up of 24 identical protein subunits and 12 haems. We have solved this structure in a tetragonal crystal form at 2.9 A resolution. We find that each haem is bound in a pocket formed by the interface between a pair of symmetry-related subunits. The quasi-twofold axis of the haem is closely aligned with the local twofold axis relating these subunits. The axial ligands of the haem are sulphurs of two equivalent methionyl residues (Met 52) from the symmetry-related subunits. A cluster of four water molecules is trapped in the gap between the upper edge of the haem and two extended protein loops which close off the haem from the outer aqueous environment. This is the first structure of a bis-methionine ligated haem-binding site and the first case of a twofold symmetric haem-binding site. |
==About this Structure== | ==About this Structure== | ||
| - | 1BCF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1BCF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Frolow, F.]] | [[Category: Frolow, F.]] | ||
| - | [[Category: Gilboa, A | + | [[Category: Gilboa, A J.Kalb.]] |
[[Category: Yariv, J.]] | [[Category: Yariv, J.]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
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[[Category: iron storage and electron transport]] | [[Category: iron storage and electron transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:47 2008'' |
Revision as of 09:53, 21 February 2008
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THE STRUCTURE OF A UNIQUE, TWO-FOLD SYMMETRIC, HAEM-BINDING SITE
Overview
Bacterioferritin of Escherichia coli, also known as cytochrome b1, is a hollow, nearly spherical shell made up of 24 identical protein subunits and 12 haems. We have solved this structure in a tetragonal crystal form at 2.9 A resolution. We find that each haem is bound in a pocket formed by the interface between a pair of symmetry-related subunits. The quasi-twofold axis of the haem is closely aligned with the local twofold axis relating these subunits. The axial ligands of the haem are sulphurs of two equivalent methionyl residues (Met 52) from the symmetry-related subunits. A cluster of four water molecules is trapped in the gap between the upper edge of the haem and two extended protein loops which close off the haem from the outer aqueous environment. This is the first structure of a bis-methionine ligated haem-binding site and the first case of a twofold symmetric haem-binding site.
About this Structure
1BCF is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of a unique twofold symmetric haem-binding site., Frolow F, Kalb AJ, Yariv J, Nat Struct Biol. 1994 Jul;1(7):453-60. PMID:7664064
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