1cxy
From Proteopedia
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|PDB= 1cxy |SIZE=350|CAPTION= <scene name='initialview01'>1cxy</scene>, resolution 1.65Å | |PDB= 1cxy |SIZE=350|CAPTION= <scene name='initialview01'>1cxy</scene>, resolution 1.65Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cxy OCA], [http://www.ebi.ac.uk/pdbsum/1cxy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cxy RCSB]</span> | ||
}} | }} | ||
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[[Category: Leys, D.]] | [[Category: Leys, D.]] | ||
[[Category: Meyer, T E.]] | [[Category: Meyer, T E.]] | ||
| - | [[Category: HEM]] | ||
[[Category: beta-strand]] | [[Category: beta-strand]] | ||
[[Category: helix]] | [[Category: helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:30:40 2008'' |
Revision as of 16:30, 30 March 2008
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| , resolution 1.65Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE AND CHARACTERIZATION OF ECTOTHIORHODOSPIRA VACUOLATA CYTOCHROME B558, A PROKARYOTIC HOMOLOGUE OF CYTOCHROME B5
Overview
A soluble cytochrome b(558) from the purple phototropic bacterium Ectothiorhodospira vacuolata was completely sequenced by a combination of automated Edman degradation and mass spectrometry. The protein, with a measured mass of 10,094.7 Da, contains 90 residues and binds a single protoheme. Unexpectedly, the sequence shows homology to eukaryotic cytochromes b(5). As no prokaryotic homologue had been reported so far, we developed a protocol for the expression, purification, and crystallization of recombinant cytochrome b(558). The structure was solved by molecular replacement to a resolution of 1.65 A. It shows that cytochrome b(558) is indeed the first bacterial cytochrome b(5) to be characterized and differs from its eukaryotic counterparts by the presence of a disulfide bridge and a four-residue insertion in front of the sixth ligand (histidine). Eukaryotes contain a variety of b(5) homologues, including soluble and membrane-bound multifunctional proteins as well as multidomain enzymes such as sulfite oxidase, fatty-acid desaturase, nitrate reductase, and lactate dehydrogenase. A search of the Mycobacterium tuberculosis genome showed that a previously unidentified gene encodes a fatty-acid desaturase with an N-terminal b(5) domain. Thus, it may provide another example of a bacterial b(5) homologue.
About this Structure
1CXY is a Single protein structure of sequence from Ectothiorhodospira shaposhnikovii. Full crystallographic information is available from OCA.
Reference
Structure and characterization of Ectothiorhodospira vacuolata cytochrome b(558), a prokaryotic homologue of cytochrome b(5)., Kostanjevecki V, Leys D, Van Driessche G, Meyer TE, Cusanovich MA, Fischer U, Guisez Y, Van Beeumen J, J Biol Chem. 1999 Dec 10;274(50):35614-20. PMID:10585439
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