2bc5: Difference between revisions
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[[Image:2bc5.gif|left|200px]] | [[Image:2bc5.gif|left|200px]] | ||
'''Crystal structure of E. coli cytochrome b562 with engineered c-type heme linkages''' | {{Structure | ||
|PDB= 2bc5 |SIZE=350|CAPTION= <scene name='initialview01'>2bc5</scene>, resolution 2.25Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of E. coli cytochrome b562 with engineered c-type heme linkages''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2BC5 is a [ | 2BC5 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=2BC5 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16939202 16939202] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
[[Category: k59w]] | [[Category: k59w]] | ||
[[Category: r98c and y101c | [[Category: r98c and y101c mutation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:00:02 2008'' | ||
Revision as of 14:00, 20 March 2008
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| 2bc5, resolution 2.25Å | |||||||||||||
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| Ligands: | SO4 and HEM | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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