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PDBsum entry 2o6t
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Crystal structure of the pa5185 protein from pseudomonas aeruginosa strain pao1- orthorhombic form (p2221).
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Structure:
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Thioesterase. Chain: a, c, e, g, i, k. Engineered: yes
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Source:
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Pseudomonas aeruginosa. Organism_taxid: 287. Gene: pa5185. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Resolution:
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2.55Å
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R-factor:
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0.183
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R-free:
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0.248
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Authors:
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M.Chruszcz,K.D.Koclega,E.Evdokimova,M.Cymborowski,M.Kudritska, A.Savchenko,A.Edwards,W.Minor
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Key ref:
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M.Chruszcz
et al.
(2008).
Function-biased choice of additives for optimization of protein crystallization - the case of the putative thioesterase PA5185 from Pseudomonas aeruginosa PAO1.
Cryst Growth Des,
8,
4054-4061.
PubMed id:
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Date:
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08-Dec-06
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Release date:
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11-Dec-07
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PROCHECK
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Headers
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References
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Q9HU04
(Q9HU04_PSEAE) -
Uncharacterized protein from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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Seq:
Struc:
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147 a.a.
146 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Cryst Growth Des
8:4054-4061
(2008)
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PubMed id:
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Function-biased choice of additives for optimization of protein crystallization - the case of the putative thioesterase PA5185 from Pseudomonas aeruginosa PAO1.
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M.Chruszcz,
M.D.Zimmerman,
S.Wang,
K.D.Koclega,
H.Zheng,
E.Evdokimova,
M.Kudritska,
M.Cymborowski,
A.Savchenko,
A.Edwards,
W.Minor.
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ABSTRACT
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The crystal structure of PA5185, a putative thioesterase from Pseudomonas
aeruginosa strain PAO1, was solved using multi-wavelength anomalous diffraction
to 2.4 A. Analysis of the structure and information about the putative function
of the protein were used to optimize crystallization conditions. The crystal
growth was optimized by applying additives with chemical similarity to a
fragment of a putative PA5185 substrate (CoA or its derivative). Using new
crystallization conditions containing this function-biased set of additives,
several new crystal forms were produced and structures of three of them (in
three different space groups) were determined. One of the new crystal forms had
an improved resolution limit of 1.9 A, and another displayed an alternative
conformation of the highly-conserved loop containing Asn26, which could play a
physiological role. Surprisingly, none of the additives were ordered in the
crystal structures. Application of function-biased additives could be used as a
standard optimization protocol for producing improved diffraction, or new
crystal forms, which may lead to better understanding of the biological
functions of proteins.
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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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M.Grabowski,
M.Chruszcz,
M.D.Zimmerman,
O.Kirillova,
and
W.Minor
(2009).
Benefits of structural genomics for drug discovery research.
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Infect Disord Drug Targets,
9,
459-474.
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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.
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Links
