Crystal structure of Campylobacter jejuni ChuZ: A split-barrel family heme oxygenase with a novel heme-binding mode

2011 ◽  
Vol 415 (1) ◽  
pp. 82-87 ◽  
Author(s):  
Rui Zhang ◽  
Jinyong Zhang ◽  
Gang Guo ◽  
Xuhu Mao ◽  
Wende Tong ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Campylobacter Jejuni ◽  
Heme Oxygenase ◽  
Binding Mode ◽  
Heme Binding

scholarly journals The Arabidopsis locus AT3G03890 encodes a dimeric β-barrel protein implicated in heme degradation

2020 ◽  
Vol 477 (24) ◽  
pp. 4785-4796
Author(s):  
Jia Wang ◽  
Qi Guo ◽  
Xiaoyi Li ◽  
Xiao Wang ◽  
Lin Liu
Keyword(s):  
Crystal Structure ◽  
Recombinant Protein ◽  
Water Molecule ◽  
Heme Oxygenase ◽  
Protein Complex ◽  
Biosynthetic Pathway ◽  
Initial Step ◽  
Heme Iron ◽  
Heme Binding ◽  
New Protein

Plant tetrapyrroles, including heme and bilins, are synthesized in plastids. Heme oxygenase (HO) catalyzes the oxidative cleavage of heme to the linear tetrapyrrole biliverdin as the initial step in bilin biosynthesis. Besides the canonical α-helical HO that is conserved from prokaryotes to human, a subfamily of non-canonical dimeric β-barrel HO has been found in bacteria. In this work, we discovered that the Arabidopsis locus AT3G03890 encodes a dimeric β-barrel protein that is structurally related to the putative non-canonical HO and is located in chloroplasts. The recombinant protein was able to bind and degrade heme in a manner different from known HO proteins. Crystal structure of the heme–protein complex reveals that the heme-binding site is in the interdimer interface and the heme iron is co-ordinated by a fixed water molecule. Our results identify a new protein that may function additionally in the tetrapyrrole biosynthetic pathway.

scholarly journals 3P005 Crystal structure of a hemophore hasA secreted by Yersinia pseudotuberclosis shows a novel heme binding mode(01A. Protein: Structure,Poster)

2013 ◽  
Vol 53 (supplement1-2) ◽  
pp. S212
Author(s):  
Masahiro Kanadani ◽  
Toshiki Muroki ◽  
Yukie Ishimaru ◽  
Saki Wada ◽  
Takehiro Sato ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Protein Structure ◽  
Binding Mode ◽  
Heme Binding

Crystal Structure of Rat Apo-Heme Oxygenase-1 (HO-1):  Mechanism of Heme Binding in HO-1 Inferred from Structural Comparison of the Apo and Heme Complex Forms†,‡

Biochemistry ◽  
2002 ◽  
Vol 41 (23) ◽  
pp. 7293-7300 ◽  
Author(s):  
Masakazu Sugishima ◽  
Hiroshi Sakamoto ◽  
Yoshimitsu Kakuta ◽  
Yoshiaki Omata ◽  
Shunsuke Hayashi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Heme Oxygenase ◽  
Heme Oxygenase 1 ◽  
Heme Binding ◽  
Structural Comparison ◽  
Complex Forms

scholarly journals The Crystal Structure of the C-Terminal Domain of the Salmonella enterica PduO Protein: An Old Fold with a New Heme-Binding Mode

2016 ◽  
Vol 7 ◽  
Author(s):  
Darío Ortiz de Orué Lucana ◽  
Neal Hickey ◽  
Michael Hensel ◽  
Johann P. Klare ◽  
Silvano Geremia ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Salmonella Enterica ◽  
Binding Mode ◽  
Heme Binding ◽  
Terminal Domain

Ruthenium(II) Complexes Bearing Thioether-Appended α- Iminopyridine Ligands: Arene Precursors Permit Access to K2-N,N and K3-N,N,S Complexes

2019 ◽  
Author(s):  
Victoria A. Ternes ◽  
Hannah A. Morgan ◽  
Austin P. Lanquist ◽  
Michael P. Murray ◽  
Bradley Wile
Keyword(s):  
Crystal Structure ◽  
Solid State ◽  
Strong Field ◽  
Active Role ◽  
Binding Mode ◽  
Phenethyl Alcohol ◽  
Ru Complexes

Herein we report the preparation of a series of Ru(II) complexes featuring alpha-iminopyridine ligands bearing thioether functionality (NNS<sup>R</sup>, where R = Me, CH<sub>2</sub>Ph, Ph). Metallation using (<i>p</i> cymene)RuCl dimer permits access to (k<sup>2</sup>-N,N)Ru complexes in which the thioether moiety remains uncoordinated. In the presence of a strong field ligand such as acetonitrile or triphenylphosphine, the p-cymene moiety is displaced, and the ligand adopts a k<sup>3</sup>-N,N,S binding mode. These complexes are characterized using a combination of solution and solid state methods, including the crystal structure of [(NNS<sup>Me</sup>)Ru(NCMe)<sub>2</sub>Cl]Cl. The k<sup>2</sup>-N,N Ru(II) complexes are shown to serve as efficient precatalysts for the oxidation of sec-phenethyl alcohol at 5 mol% loadings, using a variety of external oxidants and solvents. The complex bearing an S-Ph donor was found to be the most active of those surveyed, suggesting that the thioether donor plays an active role in catalyst speciation for this transformation.

scholarly journals Structural basis for heme-dependent NCoR binding to the transcriptional repressor REV-ERBβ

2021 ◽  
Vol 7 (5) ◽  
pp. eabc6479
Author(s):  
Sarah A. Mosure ◽  
Timothy S. Strutzenberg ◽  
Jinsai Shang ◽  
Paola Munoz-Tello ◽  
Laura A. Solt ◽  
...  
Keyword(s):  
Nuclear Receptors ◽  
Binding Mode ◽  
Structural Basis ◽  
Receptor Interaction ◽  
Heme Binding ◽  
Endogenous Ligand ◽  
Interaction Domain ◽  
Response Elements ◽  
Biochemical Assays ◽  
Chemical Cross Linking

Heme is the endogenous ligand for the constitutively repressive REV-ERB nuclear receptors, REV-ERBα (NR1D1) and REV-ERBβ (NR1D2), but how heme regulates REV-ERB activity remains unclear. Cellular studies indicate that heme is required for the REV-ERBs to bind the corepressor NCoR and repress transcription. However, fluorescence-based biochemical assays suggest that heme displaces NCoR; here, we show that this is due to a heme-dependent artifact. Using ITC and NMR spectroscopy, we show that heme binding remodels the thermodynamic interaction profile of NCoR receptor interaction domain (RID) binding to REV-ERBβ ligand-binding domain (LBD). We solved two crystal structures of REV-ERBβ LBD cobound to heme and NCoR peptides, revealing the heme-dependent NCoR binding mode. ITC and chemical cross-linking mass spectrometry reveals a 2:1 LBD:RID stoichiometry, consistent with cellular studies showing that NCoR-dependent repression of REV-ERB transcription occurs on dimeric DNA response elements. Our findings should facilitate renewed progress toward understanding heme-dependent REV-ERB activity.

scholarly journals Crystal structures of Ca2+–calmodulin bound to NaV C-terminal regions suggest role for EF-hand domain in binding and inactivation

2019 ◽  
Vol 116 (22) ◽  
pp. 10763-10772 ◽  
Author(s):  
Bernd R. Gardill ◽  
Ricardo E. Rivera-Acevedo ◽  
Ching-Chieh Tung ◽  
Filip Van Petegem
Keyword(s):  
Crystal Structure ◽  
Binding Sites ◽  
Binding Mode ◽  
Conformational Switch ◽  
Channel Inactivation ◽  
Dependent Inactivation ◽  
Ef Hand ◽  
Inherited Arrhythmia ◽  
A Site

Voltage-gated sodium (NaV) and calcium channels (CaV) form targets for calmodulin (CaM), which affects channel inactivation properties. A major interaction site for CaM resides in the C-terminal (CT) region, consisting of an IQ domain downstream of an EF-hand domain. We present a crystal structure of fully Ca2+-occupied CaM, bound to the CT of NaV1.5. The structure shows that the C-terminal lobe binds to a site ∼90° rotated relative to a previous site reported for an apoCaM complex with the NaV1.5 CT and for ternary complexes containing fibroblast growth factor homologous factors (FHF). We show that the binding of FHFs forces the EF-hand domain in a conformation that does not allow binding of the Ca2+-occupied C-lobe of CaM. These observations highlight the central role of the EF-hand domain in modulating the binding mode of CaM. The binding sites for Ca2+-free and Ca2+-occupied CaM contain targets for mutations linked to long-QT syndrome, a type of inherited arrhythmia. The related NaV1.4 channel has been shown to undergo Ca2+-dependent inactivation (CDI) akin to CaVs. We present a crystal structure of Ca2+/CaM bound to the NaV1.4 IQ domain, which shows a binding mode that would clash with the EF-hand domain. We postulate the relative reorientation of the EF-hand domain and the IQ domain as a possible conformational switch that underlies CDI.

scholarly journals Crystal Structure of the Streptomyces coelicolor Sortase E1 Transpeptidase Provides Insight into the Binding Mode of the Novel Class E Sorting Signal

PLoS ONE ◽  
2016 ◽  
Vol 11 (12) ◽  
pp. e0167763 ◽  
Author(s):  
Michele D. Kattke ◽  
Albert H. Chan ◽  
Andrew Duong ◽  
Danielle L. Sexton ◽  
Michael R. Sawaya ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Streptomyces Coelicolor ◽  
Binding Mode ◽  
The Novel ◽  
Sorting Signal ◽  
Insight Into ◽  
Class E
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