Related ArticlesInteraction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR.
J Am Chem Soc. 2005 Jan 19;127(2):567-75
Authors: Tepper AW, Bubacco L, Canters GW
The interaction of the monooxygenating type-3 copper enzyme Tyrosinase (Ty) from Streptomyces antibioticus with its inhibitor p-nitrophenol (pnp) was studied by paramagnetic NMR methods. The pnp binds to oxidized Ty (Ty(met)) and its halide (F(-), Cl(-)) bound derivatives with a dissociation constant in the mM range. The Cu(2) bridging halide ion is not displaced upon the binding of pnp showing that the pnp does not occupy the Cu(2) bridging position. The binding of pnp to Ty(met) or Ty(met)Cl leads to localized changes in the type-3 (Cu-His(3))(2) coordination geometry reflecting a change in the coordination of a single His residue that, still, remains coordinated to Cu. The binding of pnp to Ty(met)Cl causes a decrease in the Cu(2) magnetic exchange parameter -2J from 200 cm(-)(1) in the absence to 150 +/- 10 cm(-)(1) in the presence of pnp. From the (1)H and (2)D NMR relaxation parameters of pnp bound to Ty(met), a structural model of pnp coordination to the Ty type-3 center could be derived. The model explains the absence of hydroxylase activity in the closely related type-3 copper protein catechol oxidase. The relevance of the experimental findings toward the Ty catalytic mechanism is discussed.
13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interaction by NMR spectroscopy. Application to the CXCL12? chemokine.
13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interaction by NMR spectroscopy. Application to the CXCL12? chemokine.
13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interaction by NMR spectroscopy. Application to the CXCL12? chemokine.
J Am Chem Soc. 2011 Jun 2;
Authors: Laguri C, Sapay N, Simorre JP, Brutscher B, Imberty A, Gans P, Lortat-Jacob H
Heparan sulfate, a polysaccharide of the glycosaminoglycan family characterized by a unique level of complexity, has emerged as a key...
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06-04-2011 11:26 AM
The NMR Structure of FliK, the Trigger for the Switch of Substrate Specificity in the Flagellar Type III Secretion Apparatus.
The NMR Structure of FliK, the Trigger for the Switch of Substrate Specificity in the Flagellar Type III Secretion Apparatus.
The NMR Structure of FliK, the Trigger for the Switch of Substrate Specificity in the Flagellar Type III Secretion Apparatus.
J Mol Biol. 2011 Apr 12;
Authors: Mizuno S, Amida H, Kobayashi N, Aizawa SI, Tate SI
The flagellar cytoplasmic protein FliK controls hook elongation by two successive events: by determining hook length and by stopping the supply of hook protein. These two distinct roles are assigned to different...
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04-25-2011 11:53 AM
[NMR paper] A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
Related Articles A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
J Biol Chem. 2005 Nov 18;280(46):38259-63
Authors: Banci L, Bertini I, Cantini F, Chasapis CT, Hadjiliadis N, Rosato A
ATP7A is a P-type ATPase involved in copper(I) homeostasis in humans. It possesses a long N-terminal tail protruding into the cytosol and containing six...
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12-01-2010 06:56 PM
[NMR paper] An NMR study of the interaction between the human copper(I) chaperone and the second
An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.
Related Articles An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.
FEBS J. 2005 Feb;272(3):865-71
Authors: Banci L, Bertini I, Ciofi-Baffoni S, Chasapis CT, Hadjiliadis N, Rosato A
The interaction between the human copper(I) chaperone, HAH1, and one of its two physiological partners, the Menkes disease protein...
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11-24-2010 11:14 PM
[NMR paper] Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II),
Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II), and zinc(II): NMR and EPR studies.
Related Articles Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II), and zinc(II): NMR and EPR studies.
J Am Chem Soc. 2005 Jan 26;127(3):996-1006
Authors: Gaggelli E, Bernardi F, Molteni E, Pogni R, Valensin D, Valensin G, Remelli M, Luczkowski M, Kozlowski H
The synthetic peptide encompassing residues 106-126 (PrP106-126, KTNMKHMAGAAAAGAVVGGLG) of the human prion protein was considered for...
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11-24-2010 11:14 PM
[NMR paper] Interaction between an amantadine analogue and the transmembrane portion of the influ
Interaction between an amantadine analogue and the transmembrane portion of the influenza A M2 protein in liposomes probed by 1H NMR spectroscopy of the ligand.
Related Articles Interaction between an amantadine analogue and the transmembrane portion of the influenza A M2 protein in liposomes probed by 1H NMR spectroscopy of the ligand.
J Med Chem. 2004 Sep 23;47(20):4975-8
Authors: Kolocouris A, Hansen RK, Broadhurst RW
1H NMR spectroscopy of a fluoroamantadine ligand was used to probe the pH dependence of binding to the transmembrane peptide...
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[NMR paper] A strategy for the NMR characterization of type II copper(II) proteins: the case of t
A strategy for the NMR characterization of type II copper(II) proteins: the case of the copper trafficking protein CopC from Pseudomonas Syringae.
Related Articles A strategy for the NMR characterization of type II copper(II) proteins: the case of the copper trafficking protein CopC from Pseudomonas Syringae.
J Am Chem Soc. 2003 Jun 18;125(24):7200-8
Authors: Arnesano F, Banci L, Bertini I, Felli IC, Luchinat C, Thompsett AR
CopC from Pseudomonas syringae was found to be a protein capable of binding both Cu(I) and Cu(II) at two different...
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Effect of protein structural integrity on cross-linking by tyrosinase evidenced by mu
Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear NMR spectroscopy.
Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear NMR spectroscopy.
J Biotechnol. 2010 Nov 15;
Authors: Hellman M, Mattinen ML, Fu B, Buchert J, Permi P
Enzymatic cross-linking of proteins can be catalyzed either by transferase-type enzymes, e.g., transglutaminases, or by oxidoreductases, e.g, tyrosinases or laccases. Three-dimensional structure of...
Interaction between the type-3 copper protein tyrosinase and the substrate analogue p
Linear Mode
