 |
PDBsum entry 6giw
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Plant protein
|
PDB id
|
|
|
|
6giw
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Plant protein
|
|
|
Title:
|
|
Water-soluble chlorophyll protein (wscp) from lepidium virginicum (mutation l91p) with chlorophyll-a
|
|
Structure:
|
|
Water-soluble chlorophyll protein. Chain: a, b, c, d. Engineered: yes. Mutation: yes
|
|
Source:
|
|
Lepidium virginicum. Organism_taxid: 59292. Tissue: leaf. Gene: wscp1. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693
|
|
Resolution:
|
|
|
2.80Å
|
R-factor:
|
0.236
|
R-free:
|
0.277
|
|
|
Authors:
|
|
D.M.Palm,A.Agostini,V.Averesch,P.Girr,M.Werwie,S.Takahashi,H.Satoh, E.Jaenicke,H.Paulsen
|
|
Key ref:
|
|
D.M.Palm
et al.
(2018).
Chlorophyll a/b binding-specificity in water-soluble chlorophyll protein.
Nat Plants,
4,
920-929.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
15-May-18
|
Release date:
|
17-Oct-18
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
O04797
(O04797_LEPVR) -
Water-soluble chlorophyll protein from Lepidium virginicum
|
|
|
|
Seq:
Struc:
|
|
|
|
223 a.a.
156 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
|
*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Nat Plants
4:920-929
(2018)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Chlorophyll a/b binding-specificity in water-soluble chlorophyll protein.
|
|
D.M.Palm,
A.Agostini,
V.Averesch,
P.Girr,
M.Werwie,
S.Takahashi,
H.Satoh,
E.Jaenicke,
H.Paulsen.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
We altered the chlorophyll (Chl) binding sites in various versions of
water-soluble chlorophyll protein (WSCP) by amino acid exchanges to alter their
preferences for either Chl a or Chl b. WSCP is ideally suited for this
mutational analysis since it forms a tetrameric complex with only four identical
Chl binding sites. A loop of 4-6 amino acids is responsible for Chl a versus Chl
b selectivity. We show that a single amino acid exchange within this loop
changes the relative Chl a/b affinities by a factor of 40. We obtained crystal
structures of this WSCP variant binding either Chl a or Chl b. The Chl binding
sites in these structures were compared with those in the major light-harvesting
complex (LHCII) of the photosynthetic apparatus in plants to search for similar
structural features involved in Chl a/b binding specificity.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
