... 2006)
doi:10.1111/j.1742-4658.2006.05157.x
The nuclear gene MRS2 in Saccharomyces cerevisiae encodes an integral
protein (Mrs2p) of the inner mitochondrial membrane. It forms an ion
channel mediating in ux of Mg
2+
into mitochondria. ... feature of Mrs2p is the existence
of two transmembrane -domains and a short connect-
ing sequence of about 7–8 amino acids. Thi...
... linkage of the active
site Ser of the protease to the carboxyl group of P
1
by an
ester bond and insertion of the N-terminal part of the RCL
as strand 4 in b-sheet A (s4A) of the serpin. Consequently,
the ... behaviour of the serpin.
Complex formation between serpins and their cognate
proteases is fuelled by the thermodynamic properties of the
serpin. Acc...
... intermediate of NO synthesis [26]. On the other
hand, in contrast with Asn130 in arginase I, the corres-
ponding Asn149 of arginase II was not found to be a
ligand for the a-carboxylate group of the transition
state ... ligand for the a-carboxyl
group of arginine in arginase I [9,23,24]. On this basis,
direct repulsion of the negatively charged Asp130
would explain...
... bound in the binding poc ket o f a nother e nzyme
molecule within the active homomultimer. This could explain the distance in sequence homology with NRPSs C -domains displayed in the
alignment of the ... [5]. Furthermore, a chromosomal point
mutatio n in srfA-B, changing a D to A in the His-motif
(italic) of the corresponding Asp domain of the surfactin
synthe...
... shortened linker in the
mutant enzyme destabilized the interaction between
the COOH-terminal and core domains, enabling the
COOH-terminal domain of one protein to occupy its
binding site in the core ... second DNA-binding site on the protein. Fourth,
clusters of basic residues in core subdomain III, and
the linker on the side of the protein distal from the...
... removal of short acyl
chains originating from aberrant decarboxylation of chain
extender units from the thiol moiety of the 4¢-Ppant
cofactors of acyl carrier proteins [15,16]. In NRPSs there
is ... acetyl-S-Ppant-PCP. Interestingly, after 5–10 min of
incubation at 37 °C, no further hydrolysis of the remain-
ing substrate was observed, indicating clear instability of
thi...
... all the genes
involved in the pathway in the same operon; the cell
can then respond quickly to changes in the environ-
ment by changing the expression of only a few genes
and using the protein- synthesizing ... by the second gene in the las operon (Fig. 1).
In order to obtain strains with increased PK activity an
additional copy of the pyk gene was recombine...
... December
2010)
doi:10.1111/j.1742-4658.2010.07986.x
The ibuprofen primary binding site FA3–FA4 is located in domain III of
human serum albumin (HSA), the secondary clefts FA2 and FA6 being
sited in domains I and II. Here, the thermodynamics of ... effects,
combining the actions of ibuprofen and warfarin [8].
It is worth noting that the modular architecture of
HSA allow...
... rearrangement of the protein during the
docking to the binding site on the ribosome or other
ligands. Strikingly, the second most flexible part of the
protein (if one does not take into account the N-termi-
nal ... coli in vivo can be explained
by their competitive inhibition at the ribosome-binding
site [32].
Together, the M and C domains of human eRF1, in
t...
... number of RC-101 binding conforma-
tions. Docking of RC-101 to HR1 alone did not result
in a strong binding energy [Fig. 2]. Conversely, the
minimum energy of binding to HR2 is predominantly
lower ... binding of RC-101 to HR1 and the specific
binding to HR2 seen in this work. RC-101 binds
reversibly but with high affinity to glycoproteins and
associates with the cellular lipid...