Solution structure of the unbound, oxidized photosystem I subunit PsaC, containing [4Fe-4S] clusters FA and FB: A conformational change occurs upon binding to photosystem I

Mikhail L. Antonkine, Gaohua Liu, Detlef Bentrop, Donald Ashley Bryant, Ivano Bertini, Claudio Luchinat, John H. Golbeck, Dietmar Stehlik

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

This work presents the three-dimensional NMR solution structure of recombinant, oxidized, unbound PsaC from Synechococcus sp. PCC 7002. Constraints are derived from homo- and heteronuclear one-, two- and three-dimensional 1H and 15N NMR data. Significant differences are outlined between the unbound PsaC structure presented here and the available X-ray structure of bound PsaC as an integral part of the whole cyanobacterial PS I complex. These differences mainly concern the arrangement of the N- and C-termini with respect to the [4Fe-4S] core domain. In the NMR solution structure of PsaC the C-terminal region assumes a disordered helical conformation, and is clearly different from the extended coil conformation, which is one of the structural elements required to anchor PsaC to the PS I core heterodimer. In solution the N-terminus of PsaC is in contact with the pre-C-terminal region but slides in between the latter and the iron-sulfur core region of the protein. Together, these features result in a concerted movement of the N-terminus and pre-C-terminal region away from the FA binding site, accompanied by a bending of the N-terminus. In comparison, the same terminal regions are positioned much closer to FA and take up an anti-parallel β-sheet arrangement in PsaC bound to PS I. The conformational changes between bound and unbound PsaC correlate with the differences reported earlier for the EPR spectra of reduced FA and FB in bound versus unbound PsaC. The observed different structural features in solution are highly relevant for unraveling the stepwise assembly process of the stromal PsaC, PsaD and PsaE subunits to the PS I core heterodimer.

Original languageEnglish (US)
Pages (from-to)461-472
Number of pages12
JournalJournal of Biological Inorganic Chemistry
Volume7
Issue number4-5
DOIs
StatePublished - Dec 1 2002

Fingerprint

Photosystem I Protein Complex
Nuclear magnetic resonance
Conformations
Synechococcus
Anchors
Sulfur
Contacts (fluid mechanics)
Paramagnetic resonance
Iron
Binding Sites
X-Rays
X rays
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Inorganic Chemistry

Cite this

@article{1ef96a28b0424a63bcfd21c6d0d7454a,
title = "Solution structure of the unbound, oxidized photosystem I subunit PsaC, containing [4Fe-4S] clusters FA and FB: A conformational change occurs upon binding to photosystem I",
abstract = "This work presents the three-dimensional NMR solution structure of recombinant, oxidized, unbound PsaC from Synechococcus sp. PCC 7002. Constraints are derived from homo- and heteronuclear one-, two- and three-dimensional 1H and 15N NMR data. Significant differences are outlined between the unbound PsaC structure presented here and the available X-ray structure of bound PsaC as an integral part of the whole cyanobacterial PS I complex. These differences mainly concern the arrangement of the N- and C-termini with respect to the [4Fe-4S] core domain. In the NMR solution structure of PsaC the C-terminal region assumes a disordered helical conformation, and is clearly different from the extended coil conformation, which is one of the structural elements required to anchor PsaC to the PS I core heterodimer. In solution the N-terminus of PsaC is in contact with the pre-C-terminal region but slides in between the latter and the iron-sulfur core region of the protein. Together, these features result in a concerted movement of the N-terminus and pre-C-terminal region away from the FA binding site, accompanied by a bending of the N-terminus. In comparison, the same terminal regions are positioned much closer to FA and take up an anti-parallel β-sheet arrangement in PsaC bound to PS I. The conformational changes between bound and unbound PsaC correlate with the differences reported earlier for the EPR spectra of reduced FA and FB in bound versus unbound PsaC. The observed different structural features in solution are highly relevant for unraveling the stepwise assembly process of the stromal PsaC, PsaD and PsaE subunits to the PS I core heterodimer.",
author = "Antonkine, {Mikhail L.} and Gaohua Liu and Detlef Bentrop and Bryant, {Donald Ashley} and Ivano Bertini and Claudio Luchinat and Golbeck, {John H.} and Dietmar Stehlik",
year = "2002",
month = "12",
day = "1",
doi = "10.1007/s00775-001-0321-3",
language = "English (US)",
volume = "7",
pages = "461--472",
journal = "Journal of Biological Inorganic Chemistry",
issn = "0949-8257",
publisher = "Springer Verlag",
number = "4-5",

}

Solution structure of the unbound, oxidized photosystem I subunit PsaC, containing [4Fe-4S] clusters FA and FB : A conformational change occurs upon binding to photosystem I. / Antonkine, Mikhail L.; Liu, Gaohua; Bentrop, Detlef; Bryant, Donald Ashley; Bertini, Ivano; Luchinat, Claudio; Golbeck, John H.; Stehlik, Dietmar.

In: Journal of Biological Inorganic Chemistry, Vol. 7, No. 4-5, 01.12.2002, p. 461-472.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Solution structure of the unbound, oxidized photosystem I subunit PsaC, containing [4Fe-4S] clusters FA and FB

T2 - A conformational change occurs upon binding to photosystem I

AU - Antonkine, Mikhail L.

AU - Liu, Gaohua

AU - Bentrop, Detlef

AU - Bryant, Donald Ashley

AU - Bertini, Ivano

AU - Luchinat, Claudio

AU - Golbeck, John H.

AU - Stehlik, Dietmar

PY - 2002/12/1

Y1 - 2002/12/1

N2 - This work presents the three-dimensional NMR solution structure of recombinant, oxidized, unbound PsaC from Synechococcus sp. PCC 7002. Constraints are derived from homo- and heteronuclear one-, two- and three-dimensional 1H and 15N NMR data. Significant differences are outlined between the unbound PsaC structure presented here and the available X-ray structure of bound PsaC as an integral part of the whole cyanobacterial PS I complex. These differences mainly concern the arrangement of the N- and C-termini with respect to the [4Fe-4S] core domain. In the NMR solution structure of PsaC the C-terminal region assumes a disordered helical conformation, and is clearly different from the extended coil conformation, which is one of the structural elements required to anchor PsaC to the PS I core heterodimer. In solution the N-terminus of PsaC is in contact with the pre-C-terminal region but slides in between the latter and the iron-sulfur core region of the protein. Together, these features result in a concerted movement of the N-terminus and pre-C-terminal region away from the FA binding site, accompanied by a bending of the N-terminus. In comparison, the same terminal regions are positioned much closer to FA and take up an anti-parallel β-sheet arrangement in PsaC bound to PS I. The conformational changes between bound and unbound PsaC correlate with the differences reported earlier for the EPR spectra of reduced FA and FB in bound versus unbound PsaC. The observed different structural features in solution are highly relevant for unraveling the stepwise assembly process of the stromal PsaC, PsaD and PsaE subunits to the PS I core heterodimer.

AB - This work presents the three-dimensional NMR solution structure of recombinant, oxidized, unbound PsaC from Synechococcus sp. PCC 7002. Constraints are derived from homo- and heteronuclear one-, two- and three-dimensional 1H and 15N NMR data. Significant differences are outlined between the unbound PsaC structure presented here and the available X-ray structure of bound PsaC as an integral part of the whole cyanobacterial PS I complex. These differences mainly concern the arrangement of the N- and C-termini with respect to the [4Fe-4S] core domain. In the NMR solution structure of PsaC the C-terminal region assumes a disordered helical conformation, and is clearly different from the extended coil conformation, which is one of the structural elements required to anchor PsaC to the PS I core heterodimer. In solution the N-terminus of PsaC is in contact with the pre-C-terminal region but slides in between the latter and the iron-sulfur core region of the protein. Together, these features result in a concerted movement of the N-terminus and pre-C-terminal region away from the FA binding site, accompanied by a bending of the N-terminus. In comparison, the same terminal regions are positioned much closer to FA and take up an anti-parallel β-sheet arrangement in PsaC bound to PS I. The conformational changes between bound and unbound PsaC correlate with the differences reported earlier for the EPR spectra of reduced FA and FB in bound versus unbound PsaC. The observed different structural features in solution are highly relevant for unraveling the stepwise assembly process of the stromal PsaC, PsaD and PsaE subunits to the PS I core heterodimer.

UR - http://www.scopus.com/inward/record.url?scp=0036937027&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036937027&partnerID=8YFLogxK

U2 - 10.1007/s00775-001-0321-3

DO - 10.1007/s00775-001-0321-3

M3 - Article

C2 - 11941504

AN - SCOPUS:0036937027

VL - 7

SP - 461

EP - 472

JO - Journal of Biological Inorganic Chemistry

JF - Journal of Biological Inorganic Chemistry

SN - 0949-8257

IS - 4-5

ER -