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PDBsum entry 1psf
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Photosystem i
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PDB id
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1psf
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Contents |
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* Residue conservation analysis
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DOI no:
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Biochemistry
33:6052-6062
(1994)
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PubMed id:
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Three-dimensional solution structure of PsaE from the cyanobacterium Synechococcus sp. strain PCC 7002, a photosystem I protein that shows structural homology with SH3 domains.
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C.J.Falzone,
Y.H.Kao,
J.Zhao,
D.A.Bryant,
J.T.Lecomte.
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ABSTRACT
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PsaE is a 69 amino acid polypeptide from photosystem I present on the stromal
side of the thylakoid membrane. The three-dimensional solution structure of this
protein from the cyanobacterium Synechococcus sp. strain PCC 7002 was determined
at pH 5.8 and room temperature using over 900 experimental restraints derived
from two- and three-dimensional NMR experiments. The structure is comprised of a
well-defined five-stranded beta-sheet with (+1, +1, +1, -4 alpha) topology.
There is no helical region except for a single turn of 3(10) helix between the
beta D and beta E strands. PsaE also exhibits a large unrestrained loop spanning
residues 42-56. A comparison to known protein structures revealed similarity
with the Src homology 3 (SH3) domain, a membrane-associated protein involved in
signal transduction in eukaryotes. The match is remarkable as 47 of the
alpha-carbons of PsaE can be superimposed onto those of the SH3 domain from
chicken brain alpha-spectrin with a root-mean-square deviation of 2.3 A.
Although the amino acid sequences have low identity and the loops are different
in both proteins, the topology of the beta-sheet and the 3(10) turn is
conserved. SH3 domains from other sources show a similar structural homology.
The structure of PsaE was used to suggest approaches for elucidating its roles
within photosystem I.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.Niklas,
O.Gopta,
B.Epel,
W.Lubitz,
and
M.L.Antonkine
(2010).
Investigation of the Stationary and Transient A(1) Radical in Trp --> Phe Mutants of Photosystem I.
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Appl Magn Reson,
38,
187-203.
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J.A.Knappenberger,
and
J.T.Lecomte
(2007).
Loop anchor modification causes the population of an alternative native state in an SH3-like domain.
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Protein Sci,
16,
863-879.
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L.Zolla,
S.Rinalducci,
and
A.M.Timperio
(2007).
Proteomic analysis of photosystem I components from different plant species.
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Proteomics,
7,
1866-1876.
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V.Bondarenko,
S.Dewilde,
L.Moens,
and
G.N.La Mar
(2006).
Solution 1H NMR characterization of the axial bonding of the two His in oxidized human cytoglobin.
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J Am Chem Soc,
128,
12988-12999.
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J.A.Knappenberger,
C.M.Kraemer-Pecore,
and
J.T.Lecomte
(2004).
Insertion of the cytochrome b5 heme-binding loop into an SH3 domain. Effects on structure and stability, and clues about the cytochrome's architecture.
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Protein Sci,
13,
2899-2908.
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J.A.D'Aquino,
and
D.Ringe
(2003).
Determinants of the SRC homology domain 3-like fold.
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J Bacteriol,
185,
4081-4086.
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PDB code:
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R.Stoll,
C.Renner,
R.Buettner,
W.Voelter,
A.K.Bosserhoff,
and
T.A.Holak
(2003).
Backbone dynamics of the human MIA protein studied by (15)N NMR relaxation: implications for extended interactions of SH3 domains.
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Protein Sci,
12,
510-519.
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A.Lushy,
L.Verchovsky,
and
R.Nechushtai
(2002).
The stable assembly of newly synthesized PsaE into the photosystem I complex occurring via the exchange mechanism is facilitated by electrostatic interactions.
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Biochemistry,
41,
11192-11199.
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G.S.Heffelfinger,
A.Martino,
A.Gorin,
Y.Xu,
M.D.Rintoul,
A.Geist,
H.M.Al-Hashimi,
G.S.Davidson,
J.L.Faulon,
L.J.Frink,
D.M.Haaland,
W.E.Hart,
E.Jakobsson,
T.Lane,
M.Li,
P.Locascio,
F.Olken,
V.Olman,
B.Palenik,
S.J.Plimpton,
D.C.Roe,
N.F.Samatova,
M.Shah,
A.Shoshoni,
C.E.Strauss,
E.V.Thomas,
J.A.Timlin,
and
D.Xu
(2002).
Carbon sequestration in Synechococcus Sp.: from molecular machines to hierarchical modeling.
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OMICS,
6,
305-330.
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H.Delbrück,
G.Ziegelin,
E.Lanka,
and
U.Heinemann
(2002).
An Src homology 3-like domain is responsible for dimerization of the repressor protein KorB encoded by the promiscuous IncP plasmid RP4.
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J Biol Chem,
277,
4191-4198.
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PDB codes:
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V.Grantcharova,
E.J.Alm,
D.Baker,
and
A.L.Horwich
(2001).
Mechanisms of protein folding.
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Curr Opin Struct Biol,
11,
70-82.
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L.Zolla,
and
A.M.Timperio
(2000).
High performance liquid chromatography-electrospray mass spectrometry for the simultaneous resolution and identification of intrinsic thylakoid membrane proteins.
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Proteins,
41,
398-406.
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P.Barth,
I.Guillouard,
P.Sétif,
and
B.Lagoutte
(2000).
Essential role of a single arginine of photosystem I in stabilizing the electron transfer complex with ferredoxin.
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J Biol Chem,
275,
7030-7036.
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S.Dai,
C.Schwendtmayer,
P.Schürmann,
S.Ramaswamy,
and
H.Eklund
(2000).
Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster.
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Science,
287,
655-658.
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PDB code:
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J.C.Whisstock,
and
A.M.Lesk
(1999).
SH3 domains in prokaryotes.
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Trends Biochem Sci,
24,
132-133.
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O.Klukas,
W.D.Schubert,
P.Jordan,
N.Krauss,
P.Fromme,
H.T.Witt,
and
W.Saenger
(1999).
Photosystem I, an improved model of the stromal subunits PsaC, PsaD, and PsaE.
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J Biol Chem,
274,
7351-7360.
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PDB code:
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P.Barth,
B.Lagoutte,
and
P.Sétif
(1998).
Ferredoxin reduction by photosystem I from Synechocystis sp. PCC 6803: toward an understanding of the respective roles of subunits PsaD and PsaE in ferredoxin binding.
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Biochemistry,
37,
16233-16241.
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S.Knapp,
P.T.Mattson,
P.Christova,
K.D.Berndt,
A.Karshikoff,
M.Vihinen,
C.I.Smith,
and
R.Ladenstein
(1998).
Thermal unfolding of small proteins with SH3 domain folding pattern.
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Proteins,
31,
309-319.
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J.E.Gready,
S.Ranganathan,
P.R.Schofield,
Y.Matsuo,
and
K.Nishikawa
(1997).
Predicted structure of the extracellular region of ligand-gated ion-channel receptors shows SH2-like and SH3-like domains forming the ligand-binding site.
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Protein Sci,
6,
983-998.
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J.Kruip,
P.R.Chitnis,
B.Lagoutte,
M.Rögner,
and
E.J.Boekema
(1997).
Structural organization of the major subunits in cyanobacterial photosystem 1. Localization of subunits PsaC, -D, -E, -F, and -J.
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J Biol Chem,
272,
17061-17069.
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C.J.Morton,
D.J.Pugh,
E.L.Brown,
J.D.Kahmann,
D.A.Renzoni,
and
I.D.Campbell
(1996).
Solution structure and peptide binding of the SH3 domain from human Fyn.
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Structure,
4,
705-714.
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PDB codes:
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J.H.Nugent
(1996).
Oxygenic photosynthesis. Electron transfer in photosystem I and photosystem II.
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Eur J Biochem,
237,
519-531.
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N.Krauss,
W.D.Schubert,
O.Klukas,
P.Fromme,
H.T.Witt,
and
W.Saenger
(1996).
Photosystem I at 4 A resolution represents the first structural model of a joint photosynthetic reaction centre and core antenna system.
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Nat Struct Biol,
3,
965-973.
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PDB code:
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N.Narayana,
D.A.Matthews,
E.E.Howell,
and
X.Nguyen-huu
(1995).
A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site.
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Nat Struct Biol,
2,
1018-1025.
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PDB codes:
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H.Baumann,
S.Knapp,
T.Lundbäck,
R.Ladenstein,
and
T.Härd
(1994).
Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus.
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Nat Struct Biol,
1,
808-819.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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Where a reference describes a PDB structure, the PDB
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shown on the right.
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