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PDBsum entry 1ad2
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Ribosomal protein
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PDB id
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1ad2
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Ribosomal protein
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Title:
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Ribosomal protein l1 mutant with serine 179 replaced by cysteine
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Structure:
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Ribosomal protein l1. Chain: a. Synonym: tl2. Engineered: yes. Mutation: yes
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Source:
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Thermus thermophilus. Organism_taxid: 274. Strain: vk-1. Organelle: ribosome. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
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Resolution:
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1.90Å
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R-factor:
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0.203
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R-free:
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0.270
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Authors:
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J.Unge,S.Al-Karadaghi,A.Liljas,B.-H.Jonsson,I.Eliseikina,N.Ossina, N.Nevskaya,N.Fomenkova,M.Garber,S.Nikonov
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Key ref:
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J.Unge
et al.
(1997).
A mutant form of the ribosomal protein L1 reveals conformational flexibility.
Febs Lett,
411,
53-59.
PubMed id:
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Date:
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20-Feb-97
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Release date:
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15-May-97
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PROCHECK
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Headers
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References
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P27150
(RL1_THETH) -
Large ribosomal subunit protein uL1 from Thermus thermophilus
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Seq: Struc:
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229 a.a.
224 a.a.*
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Key: |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Febs Lett
411:53-59
(1997)
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PubMed id:
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A mutant form of the ribosomal protein L1 reveals conformational flexibility.
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J.Unge,
S.Al-Karadaghi,
A.Liljas,
B.H.Jonsson,
I.Eliseikina,
N.Ossina,
N.Nevskaya,
N.Fomenkova,
M.Garber,
S.Nikonov.
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ABSTRACT
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The crystal structure of the mutant S179C of the ribosomal protein L1 from
Thermus thermophilus has been determined at 1.9 A resolution. The mutant
molecule displays a small but significant opening of the cavity between the two
domains. The domain movement seems to be facilitated by the flexibility of at
least two conserved glycines. These glycines may be necessary for the larger
conformational change needed for an induced fit mechanism upon binding RNA. The
domain movement makes a disulfide bridge possible between the incorporated
cysteines in two monomers of the mutant L1.
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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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N.Nevskaya,
S.Tishchenko,
M.Paveliev,
Y.Smolinskaya,
R.Fedorov,
W.Piendl,
Y.Nakamura,
T.Toyoda,
M.Garber,
and
S.Nikonov
(2002).
Structure of ribosomal protein L1 from Methanococcus thermolithotrophicus. Functionally important structural invariants on the L1 surface.
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Acta Crystallogr D Biol Crystallogr,
58,
1023-1029.
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PDB code:
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D.I.Svergun,
and
K.H.Nierhaus
(2000).
A map of protein-rRNA distribution in the 70 S Escherichia coli ribosome.
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J Biol Chem,
275,
14432-14439.
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N.Nevskaya,
S.Tischenko,
R.Fedorov,
S.Al-Karadaghi,
A.Liljas,
A.Kraft,
W.Piendl,
M.Garber,
and
S.Nikonov
(2000).
Archaeal ribosomal protein L1: the structure provides new insights into RNA binding of the L1 protein family.
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Structure,
8,
363-371.
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PDB code:
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R.Fedorov,
N.Nevskaya,
A.Khairullina,
S.Tishchenko,
A.Mikhailov,
M.Garber,
and
S.Nikonov
(1999).
Structure of ribosomal protein L30 from Thermus thermophilus at 1.9 A resolution: conformational flexibility of the molecule.
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Acta Crystallogr D Biol Crystallogr,
55,
1827-1833.
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PDB code:
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S.V.Nikonov,
N.A.Nevskaya,
R.V.Fedorov,
A.R.Khairullina,
S.V.Tishchenko,
A.D.Nikulin,
and
M.B.Garber
(1998).
Structural studies of ribosomal proteins.
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Biol Chem,
379,
795-805.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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