1t88

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1t88.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1t88.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1t88| PDB=1t88 | SCENE= }}
{{STRUCTURE_1t88| PDB=1t88 | SCENE= }}
-
'''Crystal Structure of the Ferrous Cytochrome P450cam (C334A)'''
+
===Crystal Structure of the Ferrous Cytochrome P450cam (C334A)===
-
==Overview==
+
<!--
-
The cytochrome P450cam active site is known to be perturbed by binding to its redox partner, putidaredoxin (Pdx). Pdx binding also enhances the camphor monooxygenation reaction (Nagano, S., Shimada, H., Tarumi, A., Hishiki, T., Kimata-Ariga, Y., Egawa, T., Suematsu, M., Park, S.-Y., Adachi, S., Shiro, Y., and Ishimura, Y. (2003) Biochemistry 42, 14507-14514). These effects are unique to Pdx because nonphysiological electron donors are unable to support camphor monooxygenation. The accompanying 1H NMR paper (Tosha, T., Yoshioka, S., Ishimori, K., and Morishima, I. (2004) J. Biol. Chem. 279, 42836-42843) shows that the conformation of active site residues, Thr-252 and Cys-357, and the substrate in the ferrous (Fe(II)) CO complex of the L358P mutant mimics that of the wild-type enzyme complexed to Pdx. To explore how these changes are transmitted from the Pdx-binding site to the active site, we have solved the crystal structures of the ferrous and ferrous-CO complex of wild-type and the L358P mutant. Comparison of these structures shows that the L358P mutation results in the movement of Arg-112, a residue known to be important for putidaredoxin binding, toward the heme. This change could optimize the Pdx-binding site leading to a higher affinity for Pdx. The mutation also pushes the heme toward the substrate and ligand binding pocket, which relocates the substrate to a position favorable for regio-selective hydroxylation. The camphor is held more firmly in place as indicated by a lower average temperature factor. Residues involved in the catalytically important proton shuttle system in the I helix are also altered by the mutation. Such conformational alterations and the enhanced reactivity of the mutant oxy complex with non-physiological electron donors suggest that Pdx binding optimizes the distal pocket for monooxygenation of camphor.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15269210}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15269210 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15269210}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Heme enzyme]]
[[Category: Heme enzyme]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:39:27 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:40:51 2008''

Revision as of 23:40, 28 July 2008

Image:1t88.png

Template:STRUCTURE 1t88

Crystal Structure of the Ferrous Cytochrome P450cam (C334A)

Template:ABSTRACT PUBMED 15269210

About this Structure

1T88 is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.

Reference

Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding., Nagano S, Tosha T, Ishimori K, Morishima I, Poulos TL, J Biol Chem. 2004 Oct 8;279(41):42844-9. Epub 2004 Jul 21. PMID:15269210

Page seeded by OCA on Tue Jul 29 02:40:51 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1t88"
Personal tools