This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1kw3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kw3.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1kw3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kw3| PDB=1kw3 | SCENE= }}
{{STRUCTURE_1kw3| PDB=1kw3 | SCENE= }}
-
'''Crystal structure of 2,3-dihydroxybiphenyal dioxygenase (BphC) at 1.45 A resolution'''
+
===Crystal structure of 2,3-dihydroxybiphenyal dioxygenase (BphC) at 1.45 A resolution===
-
==Overview==
+
<!--
-
BphC derived from Pseudomonas sp. strain KKS102 is an extradiol-cleaving catecholic dioxygenase. This enzyme contains a non-heme iron atom and plays an important role in degrading biphenyl/polychlorinated biphenyls (PCBs) in the microbe. To elucidate detailed structures of BphC reaction intermediates, crystal structures of the substrate-free form, the BphC-substrate complex, and the BphC-substrate-NO (nitric oxide) complex were determined. These crystal structures revealed (1) the binding site of the O(2) molecule in the coordination sphere and (2) conformational changes of His194 during the catalytic reaction. On the basis of these findings, we propose a catalytic mechanism for the extradiol-cleaving catecholic dioxygenase in which His194 seems to play three distinct roles. At the early stage of the catalytic reaction, His194 appears to act as a catalytic base, which likely deprotonates the hydroxyl group of the substrate. At the next stage, the protonated His194 seems to stabilize a negative charge on the O2 molecule located in the hydrophobic O2-binding cavity. Finally, protonated His194 seems to function as a proton donor, whose existence has been proposed.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12206778}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12206778 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12206778}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Uragami, Y.]]
[[Category: Uragami, Y.]]
[[Category: Four time repetitions of the beta-alpha-beta-beta-beta motif]]
[[Category: Four time repetitions of the beta-alpha-beta-beta-beta motif]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:14:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:07:38 2008''

Revision as of 08:07, 2 July 2008

Image:1kw3.png

Template:STRUCTURE 1kw3

Crystal structure of 2,3-dihydroxybiphenyal dioxygenase (BphC) at 1.45 A resolution

Template:ABSTRACT PUBMED 12206778

About this Structure

1KW3 is a Single protein structure of sequence from Pseudomonas sp.. Full crystallographic information is available from OCA.

Reference

Crystal structures of the reaction intermediate and its homologue of an extradiol-cleaving catecholic dioxygenase., Sato N, Uragami Y, Nishizaki T, Takahashi Y, Sazaki G, Sugimoto K, Nonaka T, Masai E, Fukuda M, Senda T, J Mol Biol. 2002 Aug 23;321(4):621-36. PMID:12206778

Page seeded by OCA on Wed Jul 2 11:07:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kw3"
Personal tools