A Contact Site between the Two Reaction Center Polypeptides of Photosystem II Is Involved in Photoinhibition

1991 ◽  
Vol 46 (7-8) ◽  
pp. 557-562 ◽  
Author(s):  
A. Trebst
Keyword(s):  
Amino Acid ◽  
Photosystem Ii ◽  
Reaction Center ◽  
Binding Sites ◽  
Cleavage Site ◽  
Amino Acid Sequences ◽  
Contact Site ◽  
Quinone Binding ◽  
Herbicide Binding ◽  
Sensitive Site

Abstract A new contact site between the two reaction center polypeptides D 1 and D 2 of photosystem II close to arg 238 and arg 234 respectively is proposed. The amino acid sequences involved are between the 4 th transmembrane and a connecting parallel helix. The sequence includes a tryp­ sin sensitive site in both polypeptides, the likely cleavage site in the rapid turnover of the D 1 polypeptide and part of the herbicide binding site. The contact site is oriented towards both quinone binding sites Q A and Q B. A folding of the backbone of the amino acid sequences involved is proposed.

The Three-Dimensional Structure of the Herbicide Binding Niche on the Reaction Center Polypeptides of Photosystem II

1987 ◽  
Vol 42 (6) ◽  
pp. 742-750 ◽  
Author(s):  
Achim Trebst
Keyword(s):  
Amino Acid ◽  
Photosystem Ii ◽  
Reaction Center ◽  
Three Dimensional ◽  
Chemical Compounds ◽  
Dimensional Structure ◽  
Bacterial Reaction Center ◽  
Protein Subunits ◽  
Herbicide Binding ◽  
Hydropathy Analysis

The folding through the membrane of the plastoquinone and herbicide binding protein subunits of photosystem II and the topology of the binding niche for plastoquinone and herbicides is described. The model is based on the homology in amino acid sequence and folding prediction from the hydropathy analysis of the D-1 and D-2 subunits of photosystem II to the reaction center polypeptides L and M of the bacterial reaction center. It incorporates the amino acid changes in the D-1 polypeptide in herbicide tolerant plants and those indicated by chemical tagging to be involved in Qв binding. It proposes homologous amino acids in the D-1/D-2 polypeptides to those indicated by the X-ray structure of the bacterial reaction center to be involved in Fe-, quinone- and reaction center chlorophyll-binding. The different chemical compounds known to interfere with Qв function are grouped into two families depending on their orientation in the Qв binding niche.

scholarly journals Identification, characterization and cloning of myr 1, a mammalian myosin-I.

1993 ◽  
Vol 120 (6) ◽  
pp. 1393-1403 ◽  
Author(s):  
C Ruppert ◽  
R Kroschewski ◽  
M Bähler
Keyword(s):  
Amino Acid ◽  
Light Chain ◽  
Brush Border ◽  
Binding Sites ◽  
Neuronal Development ◽  
Amino Acid Sequences ◽  
Dependent Manner ◽  
Tail Domain ◽  
Myosin I ◽  
Splice Forms

We have identified, characterized and cloned a novel mammalian myosin-I motor-molecule, called myr 1 (myosin-I from rat). Myr 1 exists in three alternative splice forms: myr 1a, myr 1b, and myr 1c. These splice forms differ in their numbers of putative calmodulin/light chain binding sites. Myr 1a-c were selectively released by ATP, bound in a nucleotide-dependent manner to F-actin and exhibited amino acid sequences characteristic of myosin-I motor domains. In addition to the motor domain, they contained a regulatory domain with up to six putative calmodulin/light chain binding sites and a tail domain. The tail domain exhibited 47% amino acid sequence identity to the brush border myosin-I tail domain, demonstrating that myr 1 is related to the only other mammalian myosin-I motor molecule that has been characterized so far. In contrast to brush border myosin-I which is expressed in mature enterocytes, myr 1 splice forms were differentially expressed in all tested tissues. Therefore, myr 1 is the first mammalian myosin-I motor molecule with a widespread tissue distribution in neonatal and adult tissues. The myr 1a splice form was preferentially expressed in neuronal tissues. Its expression was developmentally regulated during rat forebrain ontogeny and subcellular fractionation revealed an enrichment in purified growth cone particles, data consistent with a role for myr 1a in neuronal development.

Molecular Modelling of the Interaction between DCMU and the QB-Binding Site of Photosystem II

1993 ◽  
Vol 48 (3-4) ◽  
pp. 191-198 ◽  
Author(s):  
Simon P. Mackay ◽  
Patrick J. O ’Malley
Keyword(s):  
Hydrogen Bond ◽  
Photosystem Ii ◽  
Binding Site ◽  
Binding Sites ◽  
The Other ◽  
Reaction Centre ◽  
Protein Model ◽  
Intermolecular Energy ◽  
Herbicide Binding ◽  
Binding Orientations

Abstract The prefered binding orientations for the herbicide DCMU within the QB-binding site of the D 1 protein model from a photosystem II reaction centre have been determined. Calculation of the intermolecular energy between the herbicide and the binding site has been instrumental in obtaining optimum positions reinforced by experimental results from mutation studies and herbicide binding to analogous bacterial reaction centres. We have shown that two binding sites are possible, one involving a hydrogen bond to and the other to the Ser 264 residue. In both cases, which are more important for the stabilization of the interactions.

scholarly journals Identification of metal ion binding sites based on amino acid sequences

PLoS ONE ◽  
2017 ◽  
Vol 12 (8) ◽  
pp. e0183756 ◽  
Author(s):  
Xiaoyong Cao ◽  
Xiuzhen Hu ◽  
Xiaojin Zhang ◽  
Sujuan Gao ◽  
Changjiang Ding ◽  
...  
Keyword(s):  
Amino Acid ◽  
Binding Sites ◽  
Metal Ion ◽  
Amino Acid Sequences ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Ion Binding Sites ◽  
Metal Ion Binding Sites

Comparison of Naturally Occurring Vitamin K-Dependent Proteins:  Correlation of Amino Acid Sequences and Membrane Binding Properties Suggests a Membrane Contact Site†

Biochemistry ◽  
1997 ◽  
Vol 36 (17) ◽  
pp. 5120-5127 ◽  
Author(s):  
John F. McDonald ◽  
Amit M. Shah ◽  
Ruth A. Schwalbe ◽  
Walter Kisiel ◽  
Björn Dahlbäck ◽  
...  
Keyword(s):  
Amino Acid ◽  
Vitamin K ◽  
Membrane Binding ◽  
Amino Acid Sequences ◽  
Contact Site ◽  
Binding Properties ◽  
Naturally Occurring ◽  
Membrane Contact
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