Protein Science
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A structural basis for processivity
Protein Science - Tập 10 Số 9 - Trang 1699-1711 - 2001
AbstractThe structures of a number of processive enzymes have been determined
recently. These proteins remain attached to their polymeric substrates and may
perform thousands of rounds of catalysis before dissociating. Based on the
degree of enclosure of the substrate, the structures fall into two broad
categories. In one group, the substrate is partially enclosed, while in the
other class, enclos...
The ankyrin repeat as molecular architecture for protein recognition
Protein Science - Tập 13 Số 6 - Trang 1435-1448 - 2004
AbstractThe ankyrin repeat is one of the most frequently observed amino acid
motifs in protein databases. This protein–protein interaction module is involved
in a diverse set of cellular functions, and consequently, defects in ankyrin
repeat proteins have been found in a number of human diseases. Recent
biophysical, crystallographic, and NMR studies have been used to measure the
stability and defi...
Helix‐bundle membrane protein fold templates
Protein Science - Tập 8 Số 12 - Trang 2711-2719 - 1999
AbstractIn the fold recognition approach to structure prediction, a sequence is
tested for compatibility with an already known fold. For membrane proteins,
however, few folds have been determined experimentally. Here the feasibility of
computing the vast majority of likely membrane protein folds is tested. The
results indicate that conformation space can be effectively sampled for small
numbers of...
Structure of the transmembrane region of the M2 protein H+ channel
Protein Science - Tập 10 Số 11 - Trang 2241-2250 - 2001
AbstractThe transmembrane domain of the M2 protein from influenza A virus forms
a nearly uniform and ideal helix in a liquid crystalline bilayer environment.
The exposure of the hydrophilic backbone structure is minimized through uniform
hydrogen bond geometry imposed by the low dielectric lipid environment. A
high‐resolution structure of the monomer backbone and a detailed description of
its orie...
Structure of a pancreatic α‐amylase bound to a substrate analogue at 2.03 Å resolution
Protein Science - Tập 6 Số 11 - Trang 2285-2296 - 1997
AbstractThe structure of pig pancreatic α‐amylase in complex with carbohydrate
inhibitor and proteinaceous inhibitors is known but the successive events
occurring at the catalytic center still remain to be elucidated. The X‐ray
structure analysis of a crystal of pig pancreatic α‐amylase (PPA, EC 3.2.1.1.)
soaked with an enzyme‐resistant substrate analogue, methyl
4,4′‐dithio‐α‐maltotrioside, showe...
Carbohydrate binding sites in a pancreatic α‐amylase‐substrate complex, derived from X‐ray structure analysis at 2.1 Å resolution
Protein Science - Tập 4 Số 4 - Trang 747-755 - 1995
AbstractThe X‐ray structure analysis of a crystal of pig pancreatic α‐amylase
(PPA, EC 3.2.1.1.) that was soaked with the substrate maltopentaose showed
electron density corresponding to two independent carbohydrate recognition sites
on the surface of the molecule. Both binding sites are distinct from the active
site described in detail in our previous high‐resolution study of a complex
between PP...
Estimation of the number of α‐helical and β‐strand segments in proteins using circular dichroism spectroscopy
Protein Science - Tập 8 Số 2 - Trang 370-380 - 1999
AbstractA simple approach to estimate the number of α‐helical and β‐strand
segments from protein circular dichroism spectra is described. The α‐helix and
β‐sheet conformations in globular protein structures, assigned by DSSP and
STRIDE algorithms, were divided into regular and distorted fractions by
considering a certain number of terminal residues in a given α‐helix or β‐strand
segment to be dist...
Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent
Protein Science - Tập 8 Số 10 - Trang 2065-2071 - 1999
AbstractOuter membrane protein A (OmpA) of Escherichia coli is a β‐barrel
membrane protein that unfolds in 8 M urea to a random coil. OmpA refolds upon
urea dilution in the presence of certain detergents or lipids. To examine the
minimal requirements for secondary and tertiary structure formation in β‐barrel
membrane proteins, folding of OmpA was studied as a function of the hydrophobic
chain leng...
Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase
Protein Science - Tập 7 Số 6 - Trang 1380-1387 - 1998
AbstractThe crystal structure of Saccharomyces cerevisiae cytoplasmic aspartate
aminotransferase (EC 2.6.1.1) has been determined to 2.05 Å resolution in the
presence of the cofactor pyridoxal‐5′‐phosphate and the competitive inhibitor
maleate. The structure was solved by the method of molecular replacement. The
final value of the crystallographic R‐factor after refinement was 23.1% with
good geom...
Motifs and structural fold of the cofactor binding site of human glutamate decarboxylase
Protein Science - Tập 7 Số 5 - Trang 1092-1105 - 1998
AbstractThe pyridoxal‐P binding sites of the two isoforms of human glutamate
decarboxylase (GAD65 and GAD67) were modeled by using PROBE (a recently
developed algorithm for multiple sequence alignment and database searching) to
align the primary sequence of GAD with pyridoxal‐P binding proteins of known
structure. GAD's cofactor binding site is particularly interesting because GAD
activity in the ...
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