1cc5: Difference between revisions

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[[Image:1cc5.gif|left|200px]]<br /><applet load="1cc5" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1cc5.gif|left|200px]]<br /><applet load="1cc5" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1cc5, resolution 2.5Å" />

'''CRYSTAL STRUCTURE OF AZOTOBACTER CYTOCHROME C5 AT 2.5 ANGSTROMS RESOLUTION'''<br />

==Overview==

The crystal structure of cytochrome c5 from Azotobacter vinelandii has, been solved and refined to an R value of 0.29 at 2.5 A resolution. The, structure of the oxidized protein was solved using a monoclinic crystal, form. The structure was solved by multiple isomorphous replacements, re-fit to a solvent-leveled multiple isomorphous replacement map, and, refined by restrained least squares. The structure reveals monomers, associated about the crystallographic 2-fold axis by hydrophobic contacts, at the "exposed heme edge". The overall conformation for the monomer is, similar to that of Pseudomonas aeruginosa cytochrome c551. However, relative to a common heme conformation, c5 and c551 differ by an average, of 6.8 A over 82 alpha-carbon positions and the propionates of c5 are much, more exposed to solvent. The shortest heme--heme contact at the "dimer", interface is 6.3 A (Fe to Fe 16.4 A). Alignment of c5 and c551 shows that, the two cytochromes, in spite of sequence differences, have remarkably, similar charge distributions. A disulfide stacks on a tyrosine between the, N- and C-terminal helices.

The crystal structure of cytochrome c5 from Azotobacter vinelandii has been solved and refined to an R value of 0.29 at 2.5 A resolution. The structure of the oxidized protein was solved using a monoclinic crystal form. The structure was solved by multiple isomorphous replacements, re-fit to a solvent-leveled multiple isomorphous replacement map, and refined by restrained least squares. The structure reveals monomers associated about the crystallographic 2-fold axis by hydrophobic contacts at the "exposed heme edge". The overall conformation for the monomer is similar to that of Pseudomonas aeruginosa cytochrome c551. However, relative to a common heme conformation, c5 and c551 differ by an average of 6.8 A over 82 alpha-carbon positions and the propionates of c5 are much more exposed to solvent. The shortest heme--heme contact at the "dimer" interface is 6.3 A (Fe to Fe 16.4 A). Alignment of c5 and c551 shows that the two cytochromes, in spite of sequence differences, have remarkably similar charge distributions. A disulfide stacks on a tyrosine between the N- and C-terminal helices.

==About this Structure==

1CC5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] 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=1CC5 OCA].

1CC5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] 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=1CC5 OCA].

==Reference==

Line 13:

[[Category: Azotobacter vinelandii]]

[[Category: Single protein]]

[[Category: Carter, D.C.]]

[[Category: Carter, D C.]]

[[Category: Stout, C.D.]]

[[Category: Stout, C D.]]

[[Category: HEM]]

[[Category: electron transport (heme protein)]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 12:20:~~06 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:34 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1cc5.gif|left|200px]]<br /><applet load="1cc5" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1cc5.gif|left|200px]]<br /><applet load="1cc5" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1cc5, resolution 2.5&Aring;" />
 '''CRYSTAL STRUCTURE OF AZOTOBACTER CYTOCHROME C5 AT 2.5 ANGSTROMS RESOLUTION'''<br />
 ==Overview==
-The crystal structure of cytochrome c5 from Azotobacter vinelandii has, been solved and refined to an R value of 0.29 at 2.5 A resolution. The, structure of the oxidized protein was solved using a monoclinic crystal, form. The structure was solved by multiple isomorphous replacements, re-fit to a solvent-leveled multiple isomorphous replacement map, and, refined by restrained least squares. The structure reveals monomers, associated about the crystallographic 2-fold axis by hydrophobic contacts, at the "exposed heme edge". The overall conformation for the monomer is, similar to that of Pseudomonas aeruginosa cytochrome c551. However, relative to a common heme conformation, c5 and c551 differ by an average, of 6.8 A over 82 alpha-carbon positions and the propionates of c5 are much, more exposed to solvent. The shortest heme--heme contact at the "dimer", interface is 6.3 A (Fe to Fe 16.4 A). Alignment of c5 and c551 shows that, the two cytochromes, in spite of sequence differences, have remarkably, similar charge distributions. A disulfide stacks on a tyrosine between the, N- and C-terminal helices.
+The crystal structure of cytochrome c5 from Azotobacter vinelandii has been solved and refined to an R value of 0.29 at 2.5 A resolution. The structure of the oxidized protein was solved using a monoclinic crystal form. The structure was solved by multiple isomorphous replacements, re-fit to a solvent-leveled multiple isomorphous replacement map, and refined by restrained least squares. The structure reveals monomers associated about the crystallographic 2-fold axis by hydrophobic contacts at the "exposed heme edge". The overall conformation for the monomer is similar to that of Pseudomonas aeruginosa cytochrome c551. However, relative to a common heme conformation, c5 and c551 differ by an average of 6.8 A over 82 alpha-carbon positions and the propionates of c5 are much more exposed to solvent. The shortest heme--heme contact at the "dimer" interface is 6.3 A (Fe to Fe 16.4 A). Alignment of c5 and c551 shows that the two cytochromes, in spite of sequence differences, have remarkably similar charge distributions. A disulfide stacks on a tyrosine between the N- and C-terminal helices.
 ==About this Structure==
-CC5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] 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=1CC5 OCA].
+CC5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] 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=1CC5 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Azotobacter vinelandii]]
 [[Category: Single protein]]
-[[Category: Carter, D.C.]]
+[[Category: Carter, D C.]]
-[[Category: Stout, C.D.]]
+[[Category: Stout, C D.]]
 [[Category: HEM]]
 [[Category: electron transport (heme protein)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:20:06 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:34 2008''