2bc5

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[[Image:2bc5.gif|left|200px]]
[[Image:2bc5.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_2bc5", creates the "Structure Box" on the page.
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|RELATEDENTRY=[[256b|256B]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bc5 OCA], [http://www.ebi.ac.uk/pdbsum/2bc5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bc5 RCSB]</span>
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'''Crystal structure of E. coli cytochrome b562 with engineered c-type heme linkages'''
'''Crystal structure of E. coli cytochrome b562 with engineered c-type heme linkages'''
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[[Category: Tezcan, F A.]]
[[Category: Tezcan, F A.]]
[[Category: Winkler, J R.]]
[[Category: Winkler, J R.]]
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[[Category: four-helix bundle]]
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[[Category: Four-helix bundle]]
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[[Category: k59w]]
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[[Category: K59w]]
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[[Category: r98c and y101c mutation]]
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[[Category: R98c and y101c mutation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:05:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:04:12 2008''
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Revision as of 17:05, 3 May 2008

Template:STRUCTURE 2bc5

Crystal structure of E. coli cytochrome b562 with engineered c-type heme linkages


Overview

The four-helix-bundle protein fold can be constructed from a wide variety of primary amino acid sequences. Proteins with this structure are excellent candidates for investigations of the relationship between folding mechanism and topology. The folding of cytochrome b(562), a four-helix-bundle heme protein, is hampered by heme dissociation. To overcome this complication, we have engineered a variant of cytochrome b(562) (cyt c-b(562)) featuring a c-type linkage between the heme and the polypeptide chain. The replacement of the native cyt b(562) leader sequence in this protein with that of a c-type cytochrome (cyt c(556)) led to high yields of fully matured and correctly folded cyt c-b(562). We have determined the X-ray crystal structure of cyt c-b(562) at 2.25 A and characterized its physical, chemical, and folding properties. These measurements reveal that the c-type linkage does not perturb the protein fold or reduction potential of the heme group. The covalent attachment of the porphyrin to the polypeptide does, however, produce a substantial change in protein stability and folding kinetics.

About this Structure

2BC5 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Stability and folding kinetics of structurally characterized cytochrome c-b562., Faraone-Mennella J, Tezcan FA, Gray HB, Winkler JR, Biochemistry. 2006 Sep 5;45(35):10504-11. PMID:16939202 Page seeded by OCA on Sat May 3 20:05:46 2008

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