2hpd: Difference between revisions

Revision as of 18:44, 21 February 2008

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

OverviewOverview

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 StructureAbout this Structure

2HPD is a Single protein structure of sequence from Bacillus megaterium with as ligand. Active as Unspecific monooxygenase, with EC number 1.14.14.1 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's., Ravichandran KG, Boddupalli SS, Hasermann CA, Peterson JA, Deisenhofer J, Science. 1993 Aug 6;261(5122):731-6. PMID:8342039

Page seeded by OCA on Thu Feb 21 17:44:13 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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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 2.0&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''