High-resolution crystal structures of the flavoprotein NrdI in oxidized and reduced states - an unusual flavodoxin: Structural biology.
Johansson, Renzo LU ; Torrents, Eduard ; Lundin, Daniel ; Sprenger, Janina LU ; Sahlin, Margareta ; Sjöberg, Britt-Marie and Logan, Derek LU
(2010)
In The FEBS Journal
277(20).
p.4265-4277
- Abstract
- The small flavoprotein NrdI is an essential component of the class Ib ribonucleotide reductase system in many bacteria. NrdI interacts with the class Ib radical generating protein NrdF. It is suggested to be involved in the rescue of inactivated diferric centres or generation of active dimanganese centres in NrdF. Although NrdI bears a superficial resemblance to flavodoxin, its redox properties have been demonstrated to be strikingly different. In particular, NrdI is capable of two-electron reduction, whereas flavodoxins are exclusively one-electron reductants. This has been suggested to depend on a lesser destabilization of the negatively-charged hydroquinone state than in flavodoxins. We have determined the crystal structures of NrdI... (More)
- The small flavoprotein NrdI is an essential component of the class Ib ribonucleotide reductase system in many bacteria. NrdI interacts with the class Ib radical generating protein NrdF. It is suggested to be involved in the rescue of inactivated diferric centres or generation of active dimanganese centres in NrdF. Although NrdI bears a superficial resemblance to flavodoxin, its redox properties have been demonstrated to be strikingly different. In particular, NrdI is capable of two-electron reduction, whereas flavodoxins are exclusively one-electron reductants. This has been suggested to depend on a lesser destabilization of the negatively-charged hydroquinone state than in flavodoxins. We have determined the crystal structures of NrdI from Bacillus anthracis, the causative agent of anthrax, in the oxidized and semiquinone forms, at resolutions of 0.96 and 1.4 Å, respectively. These structures, coupled with analysis of all curated NrdI sequences, suggest that NrdI defines a new structural family within the flavodoxin superfamily. The conformational behaviour of NrdI in response to FMN reduction is very similar to that of flavodoxins, involving a peptide flip in a loop near the N5 atom of the flavin ring. However, NrdI is much less negatively charged than flavodoxins, which is expected to affect its redox properties significantly. Indeed, sequence analysis shows a remarkable spread in the predicted isoelectric points of NrdIs, from approximately pH 4-10. The implications of these observations for class Ib ribonucleotide reductase function are discussed. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1688305
- author
- Johansson, Renzo
LU
; Torrents, Eduard
; Lundin, Daniel
; Sprenger, Janina
LU
; Sahlin, Margareta
; Sjöberg, Britt-Marie
and Logan, Derek
LU
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- ribonucleotide reductase, crystal structure, flavodoxin, NrdI, flavin mononucleotide
- in
- The FEBS Journal
- volume
- 277
- issue
- 20
- pages
- 4265 - 4277
- publisher
- Wiley-Blackwell
- external identifiers
-
- wos:000282326600014
- pmid:20831589
- scopus:77957270576
- ISSN
- 1742-464X
- DOI
- 10.1111/j.1742-4658.2010.07815.x
- language
- English
- LU publication?
- yes
- id
- be4766ca-62d2-4813-827e-36b4ab8c0fde (old id 1688305)
- date added to LUP
- 2016-04-01 14:09:28
- date last changed
- 2022-03-21 22:28:07
@article{be4766ca-62d2-4813-827e-36b4ab8c0fde,
abstract = {{The small flavoprotein NrdI is an essential component of the class Ib ribonucleotide reductase system in many bacteria. NrdI interacts with the class Ib radical generating protein NrdF. It is suggested to be involved in the rescue of inactivated diferric centres or generation of active dimanganese centres in NrdF. Although NrdI bears a superficial resemblance to flavodoxin, its redox properties have been demonstrated to be strikingly different. In particular, NrdI is capable of two-electron reduction, whereas flavodoxins are exclusively one-electron reductants. This has been suggested to depend on a lesser destabilization of the negatively-charged hydroquinone state than in flavodoxins. We have determined the crystal structures of NrdI from Bacillus anthracis, the causative agent of anthrax, in the oxidized and semiquinone forms, at resolutions of 0.96 and 1.4 Å, respectively. These structures, coupled with analysis of all curated NrdI sequences, suggest that NrdI defines a new structural family within the flavodoxin superfamily. The conformational behaviour of NrdI in response to FMN reduction is very similar to that of flavodoxins, involving a peptide flip in a loop near the N5 atom of the flavin ring. However, NrdI is much less negatively charged than flavodoxins, which is expected to affect its redox properties significantly. Indeed, sequence analysis shows a remarkable spread in the predicted isoelectric points of NrdIs, from approximately pH 4-10. The implications of these observations for class Ib ribonucleotide reductase function are discussed.}},
author = {{Johansson, Renzo and Torrents, Eduard and Lundin, Daniel and Sprenger, Janina and Sahlin, Margareta and Sjöberg, Britt-Marie and Logan, Derek}},
issn = {{1742-464X}},
keywords = {{ribonucleotide reductase; crystal structure; flavodoxin; NrdI; flavin mononucleotide}},
language = {{eng}},
number = {{20}},
pages = {{4265--4277}},
publisher = {{Wiley-Blackwell}},
series = {{The FEBS Journal}},
title = {{High-resolution crystal structures of the flavoprotein NrdI in oxidized and reduced states - an unusual flavodoxin: Structural biology.}},
url = {{http://dx.doi.org/10.1111/j.1742-4658.2010.07815.x}},
doi = {{10.1111/j.1742-4658.2010.07815.x}},
volume = {{277}},
year = {{2010}},
}