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Form and Function in Protein Dephosphorylation
1996
Cell
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A sub-family of ranching enzymes. ...
These structures revealed a common Oregon Health Sciences University Medical School motif of a central -␣--␣- scaffold containing a di-Department of Biochemistry and Molecular Biology L224 nuclear metal ...
It is attractive to (Stuckey et al., 1994) . ...
doi:10.1016/s0092-8674(00)81356-2
pmid:8898189
fatcat:2pwajimep5gpjnav66etkzunk4
Hydrolytic catalysis and structural stabilization in a designed metalloprotein
2011
Nature Chemistry
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Here, we present an artificial metallohydrolase, which has been shown by X-ray crystallography to contain two different metal ions -a Zn(II) ion which is important for catalytic activity and a Hg(II) ion ...
Reproducing these functions in a designed protein is the ultimate challenge to our understanding of them. ...
a . ...
doi:10.1038/nchem.1201
pmid:22270627
pmcid:PMC3270697
fatcat:uelxhy2spnc4bkyknvevfboule
A ligand-induced conformational change in theyersiniaprotein tyrosine phosphatase
1995
Protein Science
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The structures of several different PTPases have revealed a conserved active site architecture in which a phosphate-binding loop, together with an invariant arginine, cradle the phosphate of a phosphotyrosine ...
We previously reported that binding of tungstate to the Yop5 l PTPase from Yersiniu induced a loop conformational change that moved aspartic acid 356 into the active site, where it can function as a general ...
oxygen of a phosphotyrosine substrate (Stuckey et al., 1994) . ...
doi:10.1002/pro.5560040924
pmid:8528087
pmcid:PMC2143214
fatcat:crbc53tly5e2lmnripm4sbn5lq
The Tail of KdsC
2009
Journal of Biological Chemistry
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B, a diagram of the specific interactions of Kdo and P i in the KdsC active site. Interatomic distances shorter than 4 Å are shown by dashed lines. ...
Here, we present a set of seven structures of tetrameric Escherichia coli KdsC (ranging from 1.4 to 3.06 Å in resolution) that model different intermediate states in its catalytic mechanism. ...
The backbones of the loops undergo a movement of several Å, e.g. the C␣ atom of Arg-78 of loop 1 moves by 3.01 Å, and the C␣ atom of Ser-100 of loop 2 moves by 4.13 Å. ...
doi:10.1074/jbc.m109.012278
pmid:19726684
pmcid:PMC2781614
fatcat:t2wyzqag7vai7jbga7ykwlq5oi
A Unique Carbohydrate Binding Domain Targets the Lafora Disease Phosphatase to Glycogen
2001
Journal of Biological Chemistry
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EPM2A encodes a 331-amino acid protein containing a carboxyl-terminal phosphatase catalytic domain. ...
(Novagen) to produce a recombinant protein with a COOH-terminal 6-histidine tag. ...
A, COS1 cells were transiently co-transfected with pEGFP-Laf and pcDNA4/Myc-GS. ...
doi:10.1074/jbc.c100686200
pmid:11739371
fatcat:istsp7ouqrb53lyyuoe2tkul2e
Switching the Chirality of the Metal Environment Alters the Coordination Mode in Designed Peptides
2009
Angewandte Chemie
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) 3 À ...
to a three-coordinate site ...
doi:10.1002/ange.200902166
fatcat:e4aqzklborgx7jnx5ezikwivxq
LplA1-dependent utilization of host lipoyl peptides enables Listeria cytosolic growth and virulence
2007
Molecular Microbiology
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Thus, the ability of L. monocytogenes and other intracellular pathogens to efficiently use host lipoyl peptides as a source of lipoate may be a requisite adaptation for life within the mammalian cell. ...
L. monocytogenes is a lipoate auxotroph and must scavenge this critical cofactor, using lipoate ligases to facilitate attachment of the lipoyl moiety to metabolic enzyme complexes. ...
Stuckey and M. X. D. O'Riordan describes how LplA1 contributes to L. monocytogenes pathogenesis.
Table 1 . 1 Strains used. ...
doi:10.1111/j.1365-2958.2007.05956.x
pmid:17908209
pmcid:PMC2367003
fatcat:kgas5yiktnb25bmvundawsywci
A Crystallographic Examination of Predisposition versus Preorganization in de Novo Designed Metalloproteins
2016
Journal of the American Chemical Society
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the orientations of Cys side chains in the 16th layer of apo-(CSL16C) 3 ; Figure S3 , the similarity of the major Cys conformer orientation in apo-(CSL16C) 3 and apo-(CSL9C) 3 structures; Figure S4 , a ...
high level of preorganization of Pen ligands toward a trigonal planar Hg(II)-binding site in 3SCC peptides; Figure S5 , an alignment of the helical backbones between Hg(II) S Zn-(II) N (GRAND-CSL16CL30H ...
This is because the interlayer spacing on going from a to d residues is smaller (~4.41 Å) than on progressing from d to a in the sequence (~4.92 Å). ...
doi:10.1021/jacs.6b07165
pmid:27532255
pmcid:PMC5242185
fatcat:n5dqieexa5cyrpixxpvnv2v3wu
Crystal Structure of Patatin-17 in Complex with Aged and Non-Aged Organophosphorus Compounds
2014
PLoS ONE
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Patatin is a non-specific plant lipase and the eponymous member of a broad class of serine hydrolases termed the patatinlike phospholipase domain containing proteins (PNPLAs). ...
Citation: Wijeyesakere SJ, Richardson RJ, Stuckey JA (2014) Crystal Structure of Patatin-17 in Complex with Aged and Non-Aged Organophosphorus Compounds. PLoS ONE 9(9): e108245. ...
a/b hydrolase fold containing a central 6stranded b-sheet sandwiched by 9 a-helices along with a catalytic center composed of a Ser77-Asp215 dyad [6] . ...
doi:10.1371/journal.pone.0108245
pmid:25248161
pmcid:PMC4172759
fatcat:u2chvabggjfs7f5nhky7w66djq
Structural Basis for the Recognition of Peptide RJPXD33 by Acyltransferases in Lipid A Biosynthesis
2014
Journal of Biological Chemistry
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To gain a fundamental understanding of the molecular basis of inhibitor binding, we determined the crystal structure of LpxA from Escherichia coli in complex with RJPXD33 at 1.9 Å resolutions. ...
Overlay of the LpxA-RJPXD33 structure with E. coli LpxD identified a complementary peptide binding pocket within LpxD and serves as a model for further biochemical characterization of RJPXD33 binding to ...
min at a distance of ϳ2 cm. ...
doi:10.1074/jbc.m114.564278
pmid:24742680
pmcid:PMC4140908
fatcat:gnjfxuo5mfaatjqv54bnwrcb5m
Switching the Chirality of the Metal Environment Alters the Coordination Mode in Designed Peptides
2009
Angewandte Chemie International Edition
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) 3 À ...
to a three-coordinate site ...
doi:10.1002/anie.200902166
pmid:19579245
pmcid:PMC3014729
fatcat:4rfk3kxjd5do3hu5dq4zcjgu7a
A Potent and Highly Efficacious Bcl-2/Bcl-xL Inhibitor
2013
Journal of Medicinal Chemistry
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Compound 32 is capable of achieving rapid, complete and durable tumor regression in vivo at a well-tolerated dose-schedule. ...
a Dean-Stark apparatus. ...
Chemistry Initially, we employed a convergent synthesis 7 (Method A) for the preparation of the target molecules. ...
doi:10.1021/jm4001105
pmid:23448298
pmcid:PMC3806060
fatcat:tu3f2hn7vrfc5ndlwcl5bg3n54
The X-ray Crystal Structures ofYersiniaTyrosine Phosphatase with Bound Tungstate and Nitrate
1996
Journal of Biological Chemistry
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These energy-minimized models are consistent with a general acid-catalyzed, in-line displacement of the phosphate moiety to Cys 403 on the enzyme, followed by attack by a nucleophilic water molecule to ...
Both an associative (bond formation preceding bond cleavage) and a dissociative (bond cleavage preceding bond formation) mechanism were modeled, but a dissociative-like mechanism is favored for steric ...
Fig. 2 was made with O and VORT, with a surface generated by GRASP (47) . Figs. 3 and 4 were made using MOLSCRIPT (48) and VORT. ...
doi:10.1074/jbc.271.31.18780
pmid:8702535
fatcat:4kwhotebwvejpiiikmklfal4v4
Expression, Characterization, and Mutagenesis of theYersinia pestisMurine Toxin, a Phospholipase D Superfamily Member
1999
Journal of Biological Chemistry
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The role of the conserved residues in catalysis was further defined by the isolation of a radiolabeled phosphoenzyme intermediate, which identified a conserved histidine residue as the nucleophile in the ...
A phospholipase D (PLD) superfamily was recently identified that contains proteins of highly diverse functions with the conserved motif HXKX 4 DX 6 G(G/S). ...
A. Orth and C. A. Worby for critical reading of the manuscript, E. B. Gottlin for helpful discussions, and J. Zhou and K. Chan for excellent technical assistance. ...
doi:10.1074/jbc.274.17.11824
pmid:10207000
fatcat:sd43dbuvlvczbcvt374iqwuwgy
d -Cysteine Ligands Control Metal Geometries within De Novo Designed Three-Stranded Coiled Coils
2017
Chemistry - A European Journal
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We examine the effect of a D-configuration cysteine within a designed L-amino acid three-stranded coiled coil in order to enforce a precise coordination number on a metal center. ...
Thus, the use of non-coded amino acids in a metal's coordination sphere promises to be a powerful tool for controlling the properties of future metalloproteins. ...
The fourth ligand is a chloride ion at a distance of 2.43 Å, giving an average Zn(II)-ligand distance of 2.2(2) Å, which is reasonable for such a binding mode. ...
doi:10.1002/chem.201700660
pmid:28384393
pmcid:PMC5518473
fatcat:rcy2onajqvffnfvzb35gaiox5i
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