NDLI: Imposing function down a (cupin)-barrel: secondary structure and metal stereochemistry in the αKG-dependent oxygenases

Please wait, while we are loading the content...

The molybdoproteome of Starkeya novella– insights into the diversity and functions of molybdenum containing proteins in response to changing growth conditions

Selenite and tellurite form mixed seleno- and tellurotrisulfides with CstR from Staphylococcus aureus

The Porphyromonas gingivalis HmuY haemophore binds gallium(iii), zinc(ii), cobalt(iii), manganese(iii), nickel(ii), and copper(ii) protoporphyrin IX but in a manner different to iron(iii) protoporphyrin IX

Co(ii)-detection does not follow K_co(_ii₎ gradient: channelling in Co(ii)-sensing

A copper hyperaccumulation phenotype correlates with pathogenesis in Cryptococcus neoformans

The BaeSR regulon is involved in defense against zinc toxicity in E. coli

Streptococcus pneumoniae requires iron for its viability and expresses two membrane proteins that bind haemoglobin and haem

Aerobic uranium immobilization by Rhodanobacter A2-61 through formation of intracellular uranium–phosphate complexes

Exposure of Bacillus subtilis to mercury induces accumulation of shorter tRNA^Cys species

Back cover

Metallomics Vol - 5 Issue - 3

Metallomics Vol - 5 Issue - 2

Imposing function down a (cupin)-barrel: secondary structure and metal stereochemistry in the αKG-dependent oxygenases

Content Provider	Royal Society of Chemistry (RSC)
Author	Taabazuing, Cornelius Y. Valliere, Meaghan A. Knapp, Michael J. Hangasky, John A.
Copyright Year	2013
Abstract	The Fe(II)/αketoglutarate (αKG) dependent oxygenases catalyze a diverse range of reactions significant in biological processes such as antibiotic biosynthesis, lipid metabolism, oxygen sensing, and DNA and RNA repair. Although functionally diverse, the eight-stranded β-barrel (cupin) and HX(D/E)XnH facial triad motifs are conserved in this super-family of enzymes. Crystal structure analysis of 25 αKG oxygenases reveals two stereoisomers of the Fe cofactor, Anti and Clock, which differ in the relative position of the exchangeable ligand position and the primary substrate. Herein, we discuss the relationship between the chemical mechanism and the secondary coordination sphere of the αKG oxygenases, within the constraints of the stereochemistry of the Fe cofactor. Sequence analysis of the cupin barrel indicates that a small subset of positions constitute the second coordination sphere, which has significant ramifications for the structure of the ferryl intermediate. The competence of both Anti and Clock stereoisomers of Fe points to a ferryl intermediate that is 5 coordinate. The small number of conserved close contacts within the active sites of αKG oxygenases can be extended to chemically related enzymes, such as the αKG-dependent halogenases SyrB2 and CytC3, and the non-αKG dependent dioxygenases isopenicillin N synthase (IPNS) and cysteine dioxygenase (CDO).
Starting Page	287
Ending Page	301
Page Count	15
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	5
Issue Number	4
Journal	Metallomics
DOI	10.1039/c3mt20153h
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Antibiotics RNA Catalytic triad Ligand DNA Cupin superfamily Cofactor (biochemistry) Cysteine dioxygenase Stereochemistry Metabolism Lipid Isopenicillin N synthase
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Imposing function down a (cupin)-barrel: secondary structure and metal stereochemistry in the αKG-dependent oxygenases

2-Oxoglutarate oxygenases are inhibited by a range of transition metals

Characterization of phytochelatin synthase produced by the primitive red alga Cyanidioschyzon merolae

Thiol dioxygenases: unique families of cupin proteins

Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the alpha/beta-hydrolase family.

Involvement of the Cys-Tyr cofactor on iron binding in the active site of human cysteine dioxygenase

Predicting the catalytic sites of isopenicillin N synthase (IPNS) related non-haem iron-dependent oxygenases and oxidases (NHIDOX) through a structural superimposition and molecular docking approach

Evolution of seed storage globulins and cupin superfamily

Cysteine dioxygenase: a robust system for regulation of cellular cysteine levels

Imposing function down a (cupin)-barrel: secondary structure and metal stereochemistry in the αKG-dependent oxygenases

Similar Documents

Imposing function down a (cupin)-barrel: secondary structure and metal stereochemistry in the αKG-dependent oxygenases

2-Oxoglutarate oxygenases are inhibited by a range of transition metals

Characterization of phytochelatin synthase produced by the primitive red alga Cyanidioschyzon merolae

Thiol dioxygenases: unique families of cupin proteins

Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the alpha/beta-hydrolase family.

Involvement of the Cys-Tyr cofactor on iron binding in the active site of human cysteine dioxygenase

Predicting the catalytic sites of isopenicillin N synthase (IPNS) related non-haem iron-dependent oxygenases and oxidases (NHIDOX) through a structural superimposition and molecular docking approach

Evolution of seed storage globulins and cupin superfamily

Cysteine dioxygenase: a robust system for regulation of cellular cysteine levels

Imposing function down a (cupin)-barrel: secondary structure and metal stereochemistry in the αKG-dependent oxygenases