1phc: Difference between revisions

Revision as of 15:35, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1phc.png

Template:STRUCTURE 1phc

CRYSTAL STRUCTURE OF SUBSTRATE-FREE PSEUDOMONAS PUTIDA CYTOCHROME P450CRYSTAL STRUCTURE OF SUBSTRATE-FREE PSEUDOMONAS PUTIDA CYTOCHROME P450

Template:ABSTRACT PUBMED 3768350

About this StructureAbout this Structure

1PHC is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of substrate-free Pseudomonas putida cytochrome P-450., Poulos TL, Finzel BC, Howard AJ, Biochemistry. 1986 Sep 9;25(18):5314-22. PMID:3768350

Page seeded by OCA on Mon Jul 28 15:35:51 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1phc.gif|left|200px]]
+{{Seed}}
+[[Image:1phc.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1phc|  PDB=1phc  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF SUBSTRATE-FREE PSEUDOMONAS PUTIDA CYTOCHROME P450'''
+===CRYSTAL STRUCTURE OF SUBSTRATE-FREE PSEUDOMONAS PUTIDA CYTOCHROME P450===
-==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 line below this paragraph, {{ABSTRACT_PUBMED_3768350}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 3768350 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_3768350}}
 ==About this Structure==
@@ Line 24: / Line 28: @@
 [[Category: Single protein]]
 [[Category: Poulos, T L.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:05:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:35:51 2008''