 |
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Oxidoreductase
|
PDB id
|
|
|
|
3cxk
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
PDB id:
|
 |
|
 |
| Name: |
 |
Oxidoreductase
|
 |
|
Title:
|
 |
1.7 a crystal structure of methionine-r-sulfoxide reductase burkholderia pseudomallei: crystallization in a microfluidi card.
|
|
Structure:
|
 |
Methionine-r-sulfoxide reductase. Chain: a, b. Engineered: yes
|
|
Source:
|
 |
Burkholderia pseudomallei strain. Strain: 1710b. Gene: msrb, burps1710b_2458, yp_333853. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
Resolution:
|
 |
|
1.70Å
|
R-factor:
|
0.167
|
R-free:
|
0.199
|
|
|
Authors:
|
 |
S.Lovell,C.Gerdts,B.Staker,D.Craigen,L.Stewart,Accelerated Technologies Center For Gene To 3d Structure (Atcg3d),Seatt Structural Genomics Center For Infectious Disease (Ssgcid)
|
Key ref:
|
 |
C.J.Gerdts
et al.
(2008).
The plug-based nanovolume Microcapillary Protein Crystallization System (MPCS).
Acta Crystallogr D Biol Crystallogr,
64,
1116-1122.
PubMed id:
DOI:
|
 |
|
Date:
|
 |
|
24-Apr-08
|
Release date:
|
27-May-08
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
Headers
|
 |
|
|
References
|
|
|
|
|
|
|
Q3JRF0
(MSRB_BURP1) -
Peptide methionine sulfoxide reductase MsrB
|
|
|
|
Seq: Struc:
|
 |
 |
 |
143 a.a.
131 a.a.
|
|
|
|
|
|
|
 |
 |
|
|
Key: |
 |
PfamA domain |
 |
 |
 |
Secondary structure |
 |
|
|
|
|
 |
|
|
 |
 |
 |
 |
Enzyme class:
|
 |
E.C.1.8.4.12
- Peptide-methionine (R)-S-oxide reductase.
|
|
 |
 |
 |
 |
 |
Reaction:
|
 |
Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L- methionine (R)-S-oxide + thioredoxin
|
 |
 |
 |
 |
 |
Peptide-L-methionine
|
+
|
thioredoxin disulfide
|
+
|
H(2)O
|
=
|
peptide-L- methionine (R)-S-oxide
|
+
|
thioredoxin
|
|
 |
 |
 |
 |
 |
 |
 |
 |
Cofactor:
|
 |
Selenium; Zinc
|
 |
 |
 |
 |
 |
 |
 |
|
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
|
|
 |
 |
|
 |
|
 |
|
|
Gene Ontology (GO) functional annotation
|
|
|
|
 |
 |
 |
|
 |
 |
 |
 |
|
 |
|
Biological process
|
oxidation-reduction process
|
1 term
|
 |
|
Biochemical function
|
oxidoreductase activity
|
4 terms
|
 |
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
|
| |
|
DOI no:
|
Acta Crystallogr D Biol Crystallogr
64:1116-1122
(2008)
|
|
PubMed id:
|
|
|
|
|
| |
|
The plug-based nanovolume Microcapillary Protein Crystallization System (MPCS).
|
|
C.J.Gerdts,
M.Elliott,
S.Lovell,
M.B.Mixon,
A.J.Napuli,
B.L.Staker,
P.Nollert,
L.Stewart.
|
|
|
|
| |
ABSTRACT
|
|
|
| |
|
The Microcapillary Protein Crystallization System (MPCS) embodies a new
semi-automated plug-based crystallization technology which enables
nanolitre-volume screening of crystallization conditions in a plasticware format
that allows crystals to be easily removed for traditional cryoprotection and
X-ray diffraction data collection. Protein crystals grown in these plastic
devices can be directly subjected to in situ X-ray diffraction studies. The MPCS
integrates the formulation of crystallization cocktails with the preparation of
the crystallization experiments. Within microfluidic Teflon tubing or the
microfluidic circuitry of a plastic CrystalCard, approximately 10-20 nl volume
droplets are generated, each representing a microbatch-style crystallization
experiment with a different chemical composition. The entire protein sample is
utilized in crystallization experiments. Sparse-matrix screening and chemical
gradient screening can be combined in one comprehensive ;hybrid' crystallization
trial. The technology lends itself well to optimization by high-granularity
gradient screening using optimization reagents such as precipitation agents,
ligands or cryoprotectants.
|
|
|
|
|
| |
Selected figure(s)
|
|
|
| |
 |
 |
|
 |
|
 |
Figure 2.
Figure 2 MPCS components. (a) A picture of the components of
the MPCS system. (b) Screenshots of the operational modes of the
MicroPlugger software. (c) A picture of the MPCS CrystalCard
filled with dyed protein crystals. (d) A picture of the
PDMS/Teflon CrystalCard typically used for the hybrid method.
|
 |
Figure 5.
Figure 5 Methionine-R-sulfoxide reductase. (a) A
microphotograph of a methionine-R-sulfoxide reductase crystal.
(b) F[o] - F[c] OMIT map contoured at 3 for
Cys residues and a Zn ion. (c) Ribbon diagram of the NCS dimer
of methionine-R-sulfoxide reductase from Burkholderia
pseudomallei. Zinc ions are represented as gold spheres and
acetate ions in ball-and-stick representation. The structure was
deposited as PDB entry 3cxk .
|
 |
|
|
|
| |
The above figures are
reprinted
from an Open Access publication published by the IUCr:
Acta Crystallogr D Biol Crystallogr
(2008,
64,
1116-1122)
copyright 2008.
|
|
| |
Figures were
selected
by an automated process.
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
 |
| |
PubMed id
|
 |
Reference
|
 |
|
|
|
 |
L.Li,
W.Du,
and
R.F.Ismagilov
(2010).
Multiparameter screening on SlipChip used for nanoliter protein crystallization combining free interface diffusion and microbatch methods.
|
| |
J Am Chem Soc, 132,
112-119.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
M.Chruszcz,
M.Domagalski,
T.Osinski,
A.Wlodawer,
and
W.Minor
(2010).
Unmet challenges of structural genomics.
|
| |
Curr Opin Struct Biol, 20,
587-597.
|
 |
|
|
|
|
 |
C.L.Verlinde,
E.Fan,
S.Shibata,
Z.Zhang,
Z.Sun,
W.Deng,
J.Ross,
J.Kim,
L.Xiao,
T.L.Arakaki,
J.Bosch,
J.M.Caruthers,
E.T.Larson,
I.Letrong,
A.Napuli,
A.Kelly,
N.Mueller,
F.Zucker,
W.C.Van Voorhis,
E.A.Merritt,
and
W.G.Hol
(2009).
Fragment-based cocktail crystallography by the medical structural genomics of pathogenic protozoa consortium.
|
| |
Curr Top Med Chem, 9,
1678-1687.
|
 |
|
|
|
|
 |
P.J.Myler,
R.Stacy,
L.Stewart,
B.L.Staker,
W.C.Van Voorhis,
G.Varani,
and
G.W.Buchko
(2009).
The Seattle Structural Genomics Center for Infectious Disease (SSGCID).
|
| |
Infect Disord Drug Targets, 9,
493-506.
|
 |
|
|
|
|
 |
W.C.Van Voorhis,
W.G.Hol,
P.J.Myler,
and
L.J.Stewart
(2009).
The role of medical structural genomics in discovering new drugs for infectious diseases.
|
| |
PLoS Comput Biol, 5,
e1000530.
|
 |
|
 |
 |
|
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.
|
|