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.


1dlq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1dlq.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1dlq.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1dlq| PDB=1dlq | SCENE= }}
{{STRUCTURE_1dlq| PDB=1dlq | SCENE= }}
-
'''STRUCTURE OF CATECHOL 1,2-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 INHIBITED BY BOUND MERCURY'''
+
===STRUCTURE OF CATECHOL 1,2-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 INHIBITED BY BOUND MERCURY===
-
==Overview==
+
<!--
-
BACKGROUND: Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of catecholate derivatives to citric acid cycle intermediates. Catechol 1,2-dioxygenases (1, 2-CTDs) have a rudimentary design structure - a homodimer with one catalytic non-heme ferric ion per monomer, that is (alphaFe(3+))(2). This is in contrast to the archetypical intradiol dioxygenase protocatechuate 3,4-dioxygenase (3,4-PCD), which forms more diverse oligomers, such as (alphabetaFe(3+))(2-12). RESULTS: The crystal structure of 1,2-CTD from Acinetobacter sp. ADP1 (Ac 1,2-CTD) was solved by single isomorphous replacement and refined to 2.0 A resolution. The structures of the enzyme complexed with catechol and 4-methylcatechol were also determined at resolutions of 1.9 A and 1.8 A, respectively. While the characteristics of the iron ligands are similar, Ac 1,2-CTD differs from 3,4-PCDs in that only one subunit is used to fashion each active-site cavity. In addition, a novel 'helical zipper', consisting of five N-terminal helices from each subunit, forms the molecular dimer axis. Two phospholipids were unexpectedly found to bind within an 8 x 35 A hydrophobic tunnel along this axis. CONCLUSIONS: The helical zipper domain of Ac 1, 2-CTD has no equivalent in other proteins of known structure. Sequence analysis suggests the domain is a common motif in all members of the 1,2-CTD family. Complexes with catechol and 4-methylcatechol are the highest resolution complex structures to date of an intradiol dioxygenase. Furthermore, they confirm several observations seen in 3,4-PCDs, including ligand displacement upon binding exogenous ligands. The structures presented here are the first of a new family of intradiol dioxygenases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10801478}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10801478 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10801478}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Metalloprotein]]
[[Category: Metalloprotein]]
[[Category: Mixed alpha/beta structure]]
[[Category: Mixed alpha/beta structure]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:59:46 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:15:41 2008''

Revision as of 20:15, 30 June 2008

Image:1dlq.png

Template:STRUCTURE 1dlq

STRUCTURE OF CATECHOL 1,2-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 INHIBITED BY BOUND MERCURY

Template:ABSTRACT PUBMED 10801478

About this Structure

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

Reference

The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker., Vetting MW, Ohlendorf DH, Structure. 2000 Apr 15;8(4):429-40. PMID:10801478

Page seeded by OCA on Mon Jun 30 23:15:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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