C206, T107, and R278 are the crucial residues for H2O2 catalysis.

Slides:

Advertisements

Similar presentations

Javed A. Khan, Ben M. Dunn, Liang Tong Structure

Advertisements

Networks of Dynamic Allostery Regulate Enzyme Function

Type VIIa1 collagen and laminin-γ2 promote a p53 mutant/HIF-1–dependent proinvasive phenotype. Type VIIa1 collagen and laminin-γ2 promote a p53 mutant/HIF-1–dependent.

Interaction between the anti-EGFR Goldbody and sEGFR at the molecular level. Interaction between the anti-EGFR Goldbody and sEGFR at the molecular level.

SPR characterization of the specific interaction between AuNP–Pep1 and HEWL. (A) Binding of AuNPs functionalized with 20 Pep1 and different numbers of.

(A) Schematic illustration of the experimental design for the analysis of the RNase activity of MARF1 in oocytes by mutating the conserved D272 residue.

Crystal Structure of the Tandem Phosphatase Domains of RPTP LAR

Comparison of Cg-OxyR active-site pocket with previously published structures. Comparison of Cg-OxyR active-site pocket with previously published structures.

Cg-OxyR crystal structure shows a more symmetric subunit arrangement compared with the asymmetric relation between the RD and DBD homodimers of Pa-OxyR.

Transient overexpression of FveCYP707A4a delayed fruit ripening.

Cg-OxyR disulfide formation reorganizes its tetrameric conformation.

Structural Basis of Interdomain Communication in the Hsc70 Chaperone

Cg-OxyR controls catalase transcription, recovery from lag phase, survival to H2O2 stress, and H2O2 scavenging rate. Cg-OxyR controls catalase transcription,

Two functional states of human CFTR

(A) Stereoview of the active site of IspH with bound HMBPP (Green) including coordinated water at position W1 (Gray). (A) Stereoview of the active site.

Cg-OxyR oxidation decreases binding affinity and extension to the catalase promoter region. Cg-OxyR oxidation decreases binding affinity and extension.

Cg-OxyR shows rapid conformational changes upon oxidation.

Volume 9, Issue 2, Pages (February 2002)

Osimertinib and Cabozantinib Combinatorial Therapy in an EGFR-Mutant Lung Adenocarcinoma Patient with Multiple MET Secondary-Site Mutations after Resistance.

The interaction of FAM49B and Rac.

Stereoview of the structural superposition of IspH protein from E

Proposed reaction sequence initiating HMBPP reduction as it was derived from crystallographic data. Proposed reaction sequence initiating HMBPP reduction.

Volume 22, Issue 7, Pages (July 2014)

(A) NK cell cytotoxicity assays against K562, H9, and Raji target cell lines in the presence (black) and absence (white) of an anti-NKp30 antibody, clone.

Comparison of EM reconstructions and crystal structures of mAbs that bind at the GP1-GP2 interface. Comparison of EM reconstructions and crystal structures.

Postnatal lethality, pleural effusion in endothelial-specific Piezo1 cKO mice. Postnatal lethality, pleural effusion in endothelial-specific Piezo1 cKO.

Ping Wang, Katelyn A. Doxtader, Yunsun Nam Molecular Cell

The structure of the GPIb–filamin A complex

The hsv operon is required for virulence and suppresses defense responses. The hsv operon is required for virulence and suppresses defense responses. (A)

Volume 21, Issue 9, Pages (September 2013)

Volume 19, Issue 9, Pages (September 2011)

Volume 21, Issue 6, Pages (March 2006)

Hani S. Zaher, Rachel Green Molecular Cell

Allosteric Activation of DegS, a Stress Sensor PDZ Protease

Volume 16, Issue 6, Pages (December 2004)

Structure and T Cell Inhibition Properties of B7 Family Member, B7-H3

A Model for How Ribosomal Release Factors Induce Peptidyl-tRNA Cleavage in Termination of Protein Synthesis Stefan Trobro, Johan Åqvist Molecular Cell

Volume 16, Issue 2, Pages (February 2008)

Structural Basis of DNA Loop Recognition by Endonuclease V

Volume 101, Issue 4, Pages (May 2000)

Volume 17, Issue 11, Pages (November 2009)

GC analysis of V4 feedback modulations based on LFP data.

Fernando Corrêa, Jason Key, Brian Kuhlman, Kevin H. Gardner Structure

Volume 20, Issue 9, Pages (September 2012)

Volume 5, Issue 5, Pages (December 2013)

H.Peter Larsson, Fredrik Elinder Neuron

Structure-Function Analysis of Cell Adhesion by Neural (N-) Cadherin

Volume 7, Issue 4, Pages (October 1997)

Volume 66, Issue 5, Pages e3 (June 2017)

Volume 9, Issue 11, Pages (November 2001)

Volume 23, Issue 4, Pages (April 2015)

Volume 41, Issue 3, Pages (February 2011)

Aude Echalier, Celia F. Goodhew, Graham W. Pettigrew, Vilmos Fülöp

Volume 21, Issue 3, Pages (March 2013)

Volume 52, Issue 3, Pages (November 2013)

Volume 24, Issue 10, Pages (October 2016)

Volume 34, Issue 3, Pages (May 2009)

Structure of STAT6CF and N4 site DNA complex.

Crystal structure of STAT6CF-N3 complex and its comparison with STAT6CF-N4 complex structure. Crystal structure of STAT6CF-N3 complex and its comparison.

Volume 21, Issue 10, Pages (October 2014)

Structure and receptor-binding properties of SCH-C.

(A–F) FRET provides evidence for compaction.

Crystal Structure of a Smad MH1 Domain Bound to DNA

Fluorescence assays of diameter dependent cellular toxicity.

LC8 is structurally variable but conserved in sequence.

Structural Basis of Proline-Proline Peptide Bond Specificity of the Metalloprotease Zmp1 Implicated in Motility of Clostridium difficile Magdalena Schacherl,

Fig. 4 Steady-state difference SAXS, modeling of hydration layer, FFW flexibility in MD simulations, and active-site hydrogen bonding network. Steady-state.

(a) Pattern of UWHBs, represented as green segments joining paired α-carbons, for human Hb β-subunit. (a) Pattern of UWHBs, represented as green segments.

Volume 6, Issue 3, Pages (February 2014)

Volume 15, Issue 6, Pages (September 2004)

Presentation transcript:

C206, T107, and R278 are the crucial residues for H2O2 catalysis. C206, T107, and R278 are the crucial residues for H2O2 catalysis. (A) In the crystal structure of Cg-OxyRH2O2, an H2O2 molecule occupies the active-site pocket in two of the four chains present in the asymmetric unit. Displayed is one of the two the H2O2 binding environments, termed pocket A (see Crystallographic and Kinetic Evidence for H2O2 Binding and Reduction). Here, the side-chain of S206 is directed away from the active site, whereas in pocket B, the side-chain of S206 is directed into the active site. Both conformations are displayed here, with a double-headed arrow indicating the rotameric change. The hydrogen-bonding network between H2O2, two conserved water molecules, and residues of the active site is expressed in terms of interatomic distances. (B) Mutation of the active-site residues impairs H2O2 reduction and supports the crystallographic data. WT Cg-OxyR and mutant variants (C206S, T107V, T136V, H205A, R278Q) were mixed with an equimolar amount of H2O2, and the H2O2 concentration was monitored in function of time with the FOX assay reagent. The lines correspond to single exponential fittings of the H2O2 consumption (n = 3). The error bars correspond to SD. Brandán Pedre et al. PNAS doi:10.1073/pnas.1807954115 ©2018 by National Academy of Sciences