1apc

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1apc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apc OCA], [http://www.ebi.ac.uk/pdbsum/1apc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1apc RCSB]</span>
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'''SOLUTION STRUCTURE OF APOCYTOCHROME B562'''
'''SOLUTION STRUCTURE OF APOCYTOCHROME B562'''
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[[Category: Sligar, S G.]]
[[Category: Sligar, S G.]]
[[Category: Wand, A J.]]
[[Category: Wand, A J.]]
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[[Category: electron transport]]
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Revision as of 07:32, 2 May 2008

Image:1apc.gif

Template:STRUCTURE 1apc

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 Page seeded by OCA on Fri May 2 10:32:57 2008

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