1cxy
From Proteopedia
(New page: 200px<br /><applet load="1cxy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cxy, resolution 1.65Å" /> '''STRUCTURE AND CHARAC...) |
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| - | [[Image:1cxy.gif|left|200px]]<br /><applet load="1cxy" size=" | + | [[Image:1cxy.gif|left|200px]]<br /><applet load="1cxy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cxy, resolution 1.65Å" /> | caption="1cxy, resolution 1.65Å" /> | ||
'''STRUCTURE AND CHARACTERIZATION OF ECTOTHIORHODOSPIRA VACUOLATA CYTOCHROME B558, A PROKARYOTIC HOMOLOGUE OF CYTOCHROME B5'''<br /> | '''STRUCTURE AND CHARACTERIZATION OF ECTOTHIORHODOSPIRA VACUOLATA CYTOCHROME B558, A PROKARYOTIC HOMOLOGUE OF CYTOCHROME B5'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A soluble cytochrome b(558) from the purple phototropic bacterium | + | 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== | ==About this Structure== | ||
| - | 1CXY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ectothiorhodospira_shaposhnikovii Ectothiorhodospira shaposhnikovii] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1CXY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ectothiorhodospira_shaposhnikovii Ectothiorhodospira shaposhnikovii] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CXY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ectothiorhodospira shaposhnikovii]] | [[Category: Ectothiorhodospira shaposhnikovii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Beeumen, J | + | [[Category: Beeumen, J Van.]] |
| - | [[Category: Cusanovich, M | + | [[Category: Cusanovich, M A.]] |
| - | [[Category: Driessche, G | + | [[Category: Driessche, G Van.]] |
[[Category: Fischer, U.]] | [[Category: Fischer, U.]] | ||
[[Category: Guisez, Y.]] | [[Category: Guisez, Y.]] | ||
[[Category: Kostanjevecki, V.]] | [[Category: Kostanjevecki, V.]] | ||
[[Category: Leys, D.]] | [[Category: Leys, D.]] | ||
| - | [[Category: Meyer, T | + | [[Category: Meyer, T E.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: beta-strand]] | [[Category: beta-strand]] | ||
[[Category: helix]] | [[Category: helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:10:52 2008'' |
Revision as of 10:10, 21 February 2008
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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 with as ligand. 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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