1apc

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[[Image:1apc.gif|left|200px]]<br /><applet load="1apc" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1apc.gif|left|200px]]
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caption="1apc" />
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'''SOLUTION STRUCTURE OF APOCYTOCHROME B562'''<br />
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{{Structure
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|PDB= 1apc |SIZE=350|CAPTION= <scene name='initialview01'>1apc</scene>
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''SOLUTION STRUCTURE OF APOCYTOCHROME B562'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1APC is a [[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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Solution structure of apocytochrome b562., Feng Y, Sligar SG, Wand AJ, Nat Struct Biol. 1994 Jan;1(1):30-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7656004 7656004]
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Solution structure of apocytochrome b562., Feng Y, Sligar SG, Wand AJ, Nat Struct Biol. 1994 Jan;1(1):30-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7656004 7656004]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: electron transport]]
[[Category: electron transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:00:37 2008''

Revision as of 08:00, 20 March 2008


PDB ID 1apc

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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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