2bc5
From Proteopedia
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|PDB= 2bc5 |SIZE=350|CAPTION= <scene name='initialview01'>2bc5</scene>, resolution 2.25Å | |PDB= 2bc5 |SIZE=350|CAPTION= <scene name='initialview01'>2bc5</scene>, resolution 2.25Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[256b|256B]] | ||
| + | |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> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Tezcan, F A.]] | [[Category: Tezcan, F A.]] | ||
[[Category: Winkler, J R.]] | [[Category: Winkler, J R.]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: SO4]] | ||
[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
[[Category: k59w]] | [[Category: k59w]] | ||
[[Category: r98c and y101c mutation]] | [[Category: r98c and y101c mutation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:04:12 2008'' |
Revision as of 23:04, 30 March 2008
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| , resolution 2.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 256B
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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