1apc
From Proteopedia
(New page: 200px<br /><applet load="1apc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1apc" /> '''SOLUTION STRUCTURE OF APOCYTOCHROME B562'''<...) |
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| - | [[Image:1apc.gif|left|200px]]<br /><applet load="1apc" size=" | + | [[Image:1apc.gif|left|200px]]<br /><applet load="1apc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1apc" /> | caption="1apc" /> | ||
'''SOLUTION STRUCTURE OF APOCYTOCHROME B562'''<br /> | '''SOLUTION STRUCTURE OF APOCYTOCHROME B562'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The apoprotein is an important intermediate on the folding pathways of | + | The apoprotein is an important intermediate on the folding pathways of many haem proteins, yet a detailed structure of such an intermediate has remained elusive. Here we present the structure of apocytochrome b562 obtained by NMR spectroscopy. The apoprotein has a topology similar to the holoprotein. Nevertheless, significant differences in helix-helix packing between the two are evident. Much of the haem binding pocket in the apoprotein is preserved but exposed to solvent creating a large cavern. As apocytochrome b562 displays many of the physical characteristics ascribed to the molten globule state, these results help ellucidate the origin of several properties of the protein molten globule. |
==About this Structure== | ==About this Structure== | ||
| - | 1APC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1APC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Feng, Y.]] | [[Category: Feng, Y.]] | ||
| - | [[Category: Sligar, S | + | [[Category: Sligar, S G.]] |
| - | [[Category: Wand, A | + | [[Category: Wand, A J.]] |
[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:57 2008'' |
Revision as of 09:46, 21 February 2008
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SOLUTION STRUCTURE OF APOCYTOCHROME B562
Overview
The apoprotein is an important intermediate on the folding pathways of many haem proteins, yet a detailed structure of such an intermediate has remained elusive. Here we present the structure of apocytochrome b562 obtained by NMR spectroscopy. The apoprotein has a topology similar to the holoprotein. Nevertheless, significant differences in helix-helix packing between the two are evident. Much of the haem binding pocket in the apoprotein is preserved but exposed to solvent creating a large cavern. As apocytochrome b562 displays many of the physical characteristics ascribed to the molten globule state, these results help ellucidate the origin of several properties of the protein molten globule.
About this Structure
1APC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Solution structure of apocytochrome b562., Feng Y, Sligar SG, Wand AJ, Nat Struct Biol. 1994 Jan;1(1):30-5. PMID:7656004
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