2hpd: Difference between revisions

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[[Image:2hpd.jpg|left|200px]]<br /><applet load="2hpd" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2hpd.jpg|left|200px]]<br /><applet load="2hpd" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2hpd, resolution 2.0Å" />

'''CRYSTAL STRUCTURE OF HEMOPROTEIN DOMAIN OF P450BM-3, A PROTOTYPE FOR MICROSOMAL P450'S'''<br />

==Overview==

Cytochrome P450BM-3, a bacterial fatty acid monoxygenase, resembles the, eukaryotic microsomal P450's and their flavoprotein reductase in primary, structure and function. The three-dimensional structure of the hemoprotein, domain of P450BM-3 was determined by x-ray diffraction and refined to an R, factor of 16.9 percent at 2.0 angstrom resolution. The structure consists, of an alph and a beta domain. The active site heme is accessible through a, long hydrophobic channel formed primarily by the beta domain and the B', and F helices of the alpha domain. The two molecules in the asymmetric, unit differ in conformation around the substrate binding pocket., Substantial differences between P450BM-3 and P450cam, the only other P450, structure available, are observed around the substrate binding pocket and, the regions important for redox partner binding. A general mechanism for, proton transfer in P450's is also proposed.

Cytochrome P450BM-3, a bacterial fatty acid monoxygenase, resembles the eukaryotic microsomal P450's and their flavoprotein reductase in primary structure and function. The three-dimensional structure of the hemoprotein domain of P450BM-3 was determined by x-ray diffraction and refined to an R factor of 16.9 percent at 2.0 angstrom resolution. The structure consists of an alph and a beta domain. The active site heme is accessible through a long hydrophobic channel formed primarily by the beta domain and the B' and F helices of the alpha domain. The two molecules in the asymmetric unit differ in conformation around the substrate binding pocket. Substantial differences between P450BM-3 and P450cam, the only other P450 structure available, are observed around the substrate binding pocket and the regions important for redox partner binding. A general mechanism for proton transfer in P450's is also proposed.

==About this Structure==

2HPD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2HPD OCA].

2HPD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HPD OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Unspecific monooxygenase]]

[[Category: Boddupalli, S.S.]]

[[Category: Boddupalli, S S.]]

[[Category: Deisenhofer, J.]]

[[Category: Hasemann, C.A.]]

[[Category: Hasemann, C A.]]

[[Category: Peterson, J.A.]]

[[Category: Peterson, J A.]]

[[Category: Ravichandran, K.G.]]

[[Category: Ravichandran, K G.]]

[[Category: HEM]]

[[Category: oxidoreductase(oxygenase)]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 11:53:~~32 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:44:13 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2hpd.jpg|left|200px]]<br /><applet load="2hpd" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2hpd.jpg|left|200px]]<br /><applet load="2hpd" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2hpd, resolution 2.0&Aring;" />
 '''CRYSTAL STRUCTURE OF HEMOPROTEIN DOMAIN OF P450BM-3, A PROTOTYPE FOR MICROSOMAL P450'S'''<br />
 ==Overview==
-Cytochrome P450BM-3, a bacterial fatty acid monoxygenase, resembles the, eukaryotic microsomal P450's and their flavoprotein reductase in primary, structure and function. The three-dimensional structure of the hemoprotein, domain of P450BM-3 was determined by x-ray diffraction and refined to an R, factor of 16.9 percent at 2.0 angstrom resolution. The structure consists, of an alph and a beta domain. The active site heme is accessible through a, long hydrophobic channel formed primarily by the beta domain and the B', and F helices of the alpha domain. The two molecules in the asymmetric, unit differ in conformation around the substrate binding pocket., Substantial differences between P450BM-3 and P450cam, the only other P450, structure available, are observed around the substrate binding pocket and, the regions important for redox partner binding. A general mechanism for, proton transfer in P450's is also proposed.
+Cytochrome P450BM-3, a bacterial fatty acid monoxygenase, resembles the eukaryotic microsomal P450's and their flavoprotein reductase in primary structure and function. The three-dimensional structure of the hemoprotein domain of P450BM-3 was determined by x-ray diffraction and refined to an R factor of 16.9 percent at 2.0 angstrom resolution. The structure consists of an alph and a beta domain. The active site heme is accessible through a long hydrophobic channel formed primarily by the beta domain and the B' and F helices of the alpha domain. The two molecules in the asymmetric unit differ in conformation around the substrate binding pocket. Substantial differences between P450BM-3 and P450cam, the only other P450 structure available, are observed around the substrate binding pocket and the regions important for redox partner binding. A general mechanism for proton transfer in P450's is also proposed.
 ==About this Structure==
-HPD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HPD OCA].
+HPD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HPD OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Unspecific monooxygenase]]
-[[Category: Boddupalli, S.S.]]
+[[Category: Boddupalli, S S.]]
 [[Category: Deisenhofer, J.]]
-[[Category: Hasemann, C.A.]]
+[[Category: Hasemann, C A.]]
-[[Category: Peterson, J.A.]]
+[[Category: Peterson, J A.]]
-[[Category: Ravichandran, K.G.]]
+[[Category: Ravichandran, K G.]]
 [[Category: HEM]]
 [[Category: oxidoreductase(oxygenase)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:53:32 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:44:13 2008''