This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1c53

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1c53" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c53, resolution 1.8&Aring;" /> '''S-CLASS CYTOCHROMES C...)
Line 1: Line 1:
-
[[Image:1c53.jpg|left|200px]]<br /><applet load="1c53" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1c53.jpg|left|200px]]<br /><applet load="1c53" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1c53, resolution 1.8&Aring;" />
caption="1c53, resolution 1.8&Aring;" />
'''S-CLASS CYTOCHROMES C HAVE A VARIETY OF FOLDING PATTERNS: STRUCTURE OF CYTOCHROME C-553 FROM DESULFOVIBRIO VULGARIS DETERMINED BY THE MULTI-WAVELENGTH ANOMALOUS DISPERSION METHOD'''<br />
'''S-CLASS CYTOCHROMES C HAVE A VARIETY OF FOLDING PATTERNS: STRUCTURE OF CYTOCHROME C-553 FROM DESULFOVIBRIO VULGARIS DETERMINED BY THE MULTI-WAVELENGTH ANOMALOUS DISPERSION METHOD'''<br />
==Overview==
==Overview==
-
The three-dimensional structure of cytochrome c-553 isolated from, sulfate-reducing bacterium, Desulfovibrio vulgaris Miyazaki F strain, has, been determined by the multi-wavelength anomalous dispersion technique, with use of synchrotron radiation. The result shows that bacterial S-class, cytochromes c have a variety of folding patterns. The relative location of, two a-helices at amino- and carboxyl-terminals and the style of bonding to, the heme group show "cytochrome c folding," but other regions of the, structure are different from those of other cytochromes c previously, reported. The results also give useful information about the location of, sulfate-reducing bacterium on the phylogenetic tree of the bacterial, cytochromes c superfamily.
+
The three-dimensional structure of cytochrome c-553 isolated from sulfate-reducing bacterium, Desulfovibrio vulgaris Miyazaki F strain, has been determined by the multi-wavelength anomalous dispersion technique with use of synchrotron radiation. The result shows that bacterial S-class cytochromes c have a variety of folding patterns. The relative location of two a-helices at amino- and carboxyl-terminals and the style of bonding to the heme group show "cytochrome c folding," but other regions of the structure are different from those of other cytochromes c previously reported. The results also give useful information about the location of sulfate-reducing bacterium on the phylogenetic tree of the bacterial cytochromes c superfamily.
==About this Structure==
==About this Structure==
-
1C53 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C53 OCA].
+
1C53 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] 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=1C53 OCA].
==Reference==
==Reference==
-
S-class cytochromes c have a variety of folding patterns: structure of cytochrome c-553 from Desulfovibrio vulgaris determined by the multi-wavelength anomalous dispersion method., Nakagawa A, Higuchi Y, Yasuoka N, Katsube Y, Yagi T, J Biochem (Tokyo). 1990 Nov;108(5):701-3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1964450 1964450]
+
S-class cytochromes c have a variety of folding patterns: structure of cytochrome c-553 from Desulfovibrio vulgaris determined by the multi-wavelength anomalous dispersion method., Nakagawa A, Higuchi Y, Yasuoka N, Katsube Y, Yagi T, J Biochem. 1990 Nov;108(5):701-3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1964450 1964450]
[[Category: Desulfovibrio vulgaris]]
[[Category: Desulfovibrio vulgaris]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 21: Line 21:
[[Category: electron transport]]
[[Category: electron transport]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:09:53 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:02:27 2008''

Revision as of 10:02, 21 February 2008


1c53, resolution 1.8Å

Drag the structure with the mouse to rotate

S-CLASS CYTOCHROMES C HAVE A VARIETY OF FOLDING PATTERNS: STRUCTURE OF CYTOCHROME C-553 FROM DESULFOVIBRIO VULGARIS DETERMINED BY THE MULTI-WAVELENGTH ANOMALOUS DISPERSION METHOD

Overview

The three-dimensional structure of cytochrome c-553 isolated from sulfate-reducing bacterium, Desulfovibrio vulgaris Miyazaki F strain, has been determined by the multi-wavelength anomalous dispersion technique with use of synchrotron radiation. The result shows that bacterial S-class cytochromes c have a variety of folding patterns. The relative location of two a-helices at amino- and carboxyl-terminals and the style of bonding to the heme group show "cytochrome c folding," but other regions of the structure are different from those of other cytochromes c previously reported. The results also give useful information about the location of sulfate-reducing bacterium on the phylogenetic tree of the bacterial cytochromes c superfamily.

About this Structure

1C53 is a Single protein structure of sequence from Desulfovibrio vulgaris with as ligand. Full crystallographic information is available from OCA.

Reference

S-class cytochromes c have a variety of folding patterns: structure of cytochrome c-553 from Desulfovibrio vulgaris determined by the multi-wavelength anomalous dispersion method., Nakagawa A, Higuchi Y, Yasuoka N, Katsube Y, Yagi T, J Biochem. 1990 Nov;108(5):701-3. PMID:1964450

Page seeded by OCA on Thu Feb 21 12:02:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools