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PDBsum entry 1e2b
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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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Nmr structure of the c10s mutant of enzyme iib cellobiose of the phosphoenol-pyruvate dependent phosphotransferase system of escherichia coli, 17 structures
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Structure:
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Enzyme iib-cellobiose. Chain: a. Engineered: yes. Mutation: yes
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Source:
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Escherichia coli. Organism_taxid: 83333. Strain: k12. Cellular_location: cytoplasm. Gene: cela. Expressed in: escherichia coli str. K12 substr. W3110. Expression_system_taxid: 316407.
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NMR struc:
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17 models
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Authors:
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E.Ab,G.Schuurman-Wolters,J.Reizer,M.H.Saier,K.Dijkstra,R.M.Scheek, G.T.Robillard
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Key ref:
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E.Ab
et al.
(1997).
The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli.
Protein Sci,
6,
304-314.
PubMed id:
DOI:
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Date:
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15-Nov-96
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Release date:
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23-Jul-97
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PROCHECK
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Headers
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References
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P69795
(PTQB_ECOLI) -
PTS system N,N'-diacetylchitobiose-specific EIIB component from Escherichia coli (strain K12)
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Seq: Struc:
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106 a.a.
106 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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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.2.7.1.196
- protein-N(pi)-phosphohistidine--N,N'-diacetylchitobiose
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Reaction:
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N,N'-diacetylchitobiose(out) + N(pros)-phospho-L-histidyl-[protein] = diacetylchitobiose-6'-phosphate(in) + L-histidyl-[protein]
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[Protein]-N(pi)-phospho-L-histidine
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+
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N,N'-diacetylchitobiose(Side 1)
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=
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[protein]-L-histidine
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N,N'-diacetylchitobiose 6'-phosphate(Side 2)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Protein Sci
6:304-314
(1997)
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PubMed id:
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The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli.
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E.Ab,
G.Schuurman-Wolters,
J.Reizer,
M.H.Saier,
K.Dijkstra,
R.M.Scheek,
G.T.Robillard.
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ABSTRACT
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The assignment of the side-chain NMR resonances and the determination of the
three-dimensional solution structure of the C10S mutant of enzyme IIBcellobiose
(IIBcel) of the phosphoenolpyruvate-dependent phosphotransferase system of
Escherichia coli are presented. The side-chain resonances were assigned nearly
completely using a variety of mostly heteronuclear NMR experiments, including
HCCH-TOCSY, HCCH-COSY, and COCCH-TOCSY experiments as well as CBCACOHA,
CBCA(CO)NH, and HBHA(CBCA)(CO)NH experiments. In order to obtain the
three-dimensional structure, NOE data were collected from 15N-NOESY-HSQC,
13C-HSQC-NOESY, and 2D NOE experiments. The distance restraints derived from
these NOE data were used in distance geometry calculations followed by molecular
dynamics and simulated annealing protocols. In an iterative procedure,
additional NOE assignments were derived from the calculated structures and new
structures were calculated. The final set of structures, calculated with
approximately 2000 unambiguous and ambiguous distance restraints, has an rms
deviation of 1.1 A on C alpha atoms. IIBcel consists of a four stranded parallel
beta-sheet, in the order 2134. The sheet is flanked with two and three
alpha-helices on either side. Residue 10, a cysteine in the wild-type enzyme,
which is phosphorylated during the catalytic cycle, is located at the end of the
first beta-strand. A loop that is proposed to be involved in the binding of the
phosphoryl-group follows the cysteine. The loop appears to be disordered in the
unphosphorylated state.
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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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Y.S.Jung,
M.Cai,
and
G.M.Clore
(2010).
Solution structure of the IIAChitobiose-IIBChitobiose complex of the N,N'-diacetylchitobiose branch of the Escherichia coli phosphotransferase system.
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J Biol Chem,
285,
4173-4184.
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PDB codes:
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J.Deutscher,
C.Francke,
and
P.W.Postma
(2006).
How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria.
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Microbiol Mol Biol Rev,
70,
939.
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L.Volpon,
C.R.Young,
A.Matte,
and
K.Gehring
(2006).
NMR structure of the enzyme GatB of the galactitol-specific phosphoenolpyruvate-dependent phosphotransferase system and its interaction with GatA.
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Protein Sci,
15,
2435-2441.
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PDB code:
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C.L.Gustafson,
C.V.Stauffacher,
K.Hallenga,
and
R.L.Van Etten
(2005).
Solution structure of the low-molecular-weight protein tyrosine phosphatase from Tritrichomonas foetus reveals a flexible phosphate binding loop.
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Protein Sci,
14,
2515-2525.
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PDB code:
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I.Zegers,
J.C.Martins,
R.Willem,
L.Wyns,
and
J.Messens
(2001).
Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty.
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Nat Struct Biol,
8,
843-847.
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PDB codes:
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G.Wang,
J.M.Louis,
M.Sondej,
Y.J.Seok,
A.Peterkofsky,
and
G.M.Clore
(2000).
Solution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIA(glucose) of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system.
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EMBO J,
19,
5635-5649.
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PDB code:
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T.Kernebeck,
S.Pflanz,
G.Müller-Newen,
G.Kurapkat,
R.M.Scheek,
K.Dijkstra,
P.C.Heinrich,
A.Wollmer,
S.Grzesiek,
and
J.Grötzinger
(1999).
The signal transducer gp130: solution structure of the carboxy-terminal domain of the cytokine receptor homology region.
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Protein Sci,
8,
5.
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PDB code:
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P.Sliz,
R.Engelmann,
W.Hengstenberg,
and
E.F.Pai
(1997).
The structure of enzyme IIAlactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system.
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Structure,
5,
775-788.
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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
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
codes are
shown on the right.
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}
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