1phc: Difference between revisions

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

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

caption="1phc, resolution 1.6Å" />

'''CRYSTAL STRUCTURE OF SUBSTRATE-FREE PSEUDOMONAS PUTIDA CYTOCHROME P450'''<br />

==Overview==

The crystal structure of Pseudomonas putida cytochrome P-450cam in the, substrate-free form has been refined at 2.20-A resolution and compared to, the substrate-bound form of the enzyme. In the absence of the substrate, camphor, the P-450cam heme iron atom is hexacoordinate with the sulfur, atom of Cys-357 providing one axial heme ligand and a water molecule or, hydroxide ion providing the other axial ligand. A network of, hydrogen-bonded solvent molecules occupies the substrate pocket in, addition to the iron-linked aqua ligand. When a camphor molecule binds, the active site waters including the aqua ligand are displaced, resulting, in a pentacoordinate high-spin heme iron atom. Analysis of the Fno camphor, - F camphor difference Fourier and a quantitative comparison of the two, refined structures reveal that no detectable conformational change results, from camphor binding other than a small repositioning of a phenylalanine, side chain that contacts the camphor molecule. However, large decreases in, the mean temperature factors of three separate segments of the protein, centered on Tyr-96, Thr-185, and Asp-251 result from camphor binding. This, indicates that camphor binding decreases the flexibility in these three, regions of the P-450cam molecule without altering the mean position of the, atoms involved.

The crystal structure of Pseudomonas putida cytochrome P-450cam in the substrate-free form has been refined at 2.20-A resolution and compared to the substrate-bound form of the enzyme. In the absence of the substrate camphor, the P-450cam heme iron atom is hexacoordinate with the sulfur atom of Cys-357 providing one axial heme ligand and a water molecule or hydroxide ion providing the other axial ligand. A network of hydrogen-bonded solvent molecules occupies the substrate pocket in addition to the iron-linked aqua ligand. When a camphor molecule binds, the active site waters including the aqua ligand are displaced, resulting in a pentacoordinate high-spin heme iron atom. Analysis of the Fno camphor - F camphor difference Fourier and a quantitative comparison of the two refined structures reveal that no detectable conformational change results from camphor binding other than a small repositioning of a phenylalanine side chain that contacts the camphor molecule. However, large decreases in the mean temperature factors of three separate segments of the protein centered on Tyr-96, Thr-185, and Asp-251 result from camphor binding. This indicates that camphor binding decreases the flexibility in these three regions of the P-450cam molecule without altering the mean position of the atoms involved.

==About this Structure==

1PHC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1PHC OCA].

1PHC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PHC OCA].

==Reference==

Line 14:

[[Category: Pseudomonas putida]]

[[Category: Single protein]]

[[Category: Poulos, T.L.]]

[[Category: Poulos, T L.]]

[[Category: HEM]]

[[Category: oxidoreductase(oxygenase)]]

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@@ Line 1: / Line 1: @@
-[[Image:1phc.gif|left|200px]]<br /><applet load="1phc" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1phc.gif|left|200px]]<br /><applet load="1phc" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1phc, resolution 1.6&Aring;" />
 '''CRYSTAL STRUCTURE OF SUBSTRATE-FREE PSEUDOMONAS PUTIDA CYTOCHROME P450'''<br />
 ==Overview==
-The crystal structure of Pseudomonas putida cytochrome P-450cam in the, substrate-free form has been refined at 2.20-A resolution and compared to, the substrate-bound form of the enzyme. In the absence of the substrate, camphor, the P-450cam heme iron atom is hexacoordinate with the sulfur, atom of Cys-357 providing one axial heme ligand and a water molecule or, hydroxide ion providing the other axial ligand. A network of, hydrogen-bonded solvent molecules occupies the substrate pocket in, addition to the iron-linked aqua ligand. When a camphor molecule binds, the active site waters including the aqua ligand are displaced, resulting, in a pentacoordinate high-spin heme iron atom. Analysis of the Fno camphor, - F camphor difference Fourier and a quantitative comparison of the two, refined structures reveal that no detectable conformational change results, from camphor binding other than a small repositioning of a phenylalanine, side chain that contacts the camphor molecule. However, large decreases in, the mean temperature factors of three separate segments of the protein, centered on Tyr-96, Thr-185, and Asp-251 result from camphor binding. This, indicates that camphor binding decreases the flexibility in these three, regions of the P-450cam molecule without altering the mean position of the, atoms involved.
+The crystal structure of Pseudomonas putida cytochrome P-450cam in the substrate-free form has been refined at 2.20-A resolution and compared to the substrate-bound form of the enzyme. In the absence of the substrate camphor, the P-450cam heme iron atom is hexacoordinate with the sulfur atom of Cys-357 providing one axial heme ligand and a water molecule or hydroxide ion providing the other axial ligand. A network of hydrogen-bonded solvent molecules occupies the substrate pocket in addition to the iron-linked aqua ligand. When a camphor molecule binds, the active site waters including the aqua ligand are displaced, resulting in a pentacoordinate high-spin heme iron atom. Analysis of the Fno camphor - F camphor difference Fourier and a quantitative comparison of the two refined structures reveal that no detectable conformational change results from camphor binding other than a small repositioning of a phenylalanine side chain that contacts the camphor molecule. However, large decreases in the mean temperature factors of three separate segments of the protein centered on Tyr-96, Thr-185, and Asp-251 result from camphor binding. This indicates that camphor binding decreases the flexibility in these three regions of the P-450cam molecule without altering the mean position of the atoms involved.
 ==About this Structure==
-PHC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PHC OCA].
+PHC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PHC OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Pseudomonas putida]]
 [[Category: Single protein]]
-[[Category: Poulos, T.L.]]
+[[Category: Poulos, T L.]]
 [[Category: HEM]]
 [[Category: oxidoreductase(oxygenase)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:48:45 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:28:46 2008''