scholarly journals Insights revealed by the co‐crystal structure of the Saccharomyces cerevisiae histidine phosphotransfer protein Ypd1 and the receiver domain of its downstream response regulator Ssk1

2019 ◽  
Vol 28 (12) ◽  
pp. 2099-2111 ◽  
Author(s):  
Katie M. Branscum ◽  
Smita K. Menon ◽  
Clay A. Foster ◽  
Ann H. West
Keyword(s):  
Crystal Structure ◽  
Saccharomyces Cerevisiae ◽  
Response Regulator ◽  
Receiver Domain ◽  
Histidine Phosphotransfer

scholarly journals Crystal structure of nonphosphorylated receiver domain of the stress response regulator RcsB fromEscherichia coli

2016 ◽  
Vol 25 (12) ◽  
pp. 2216-2224 ◽  
Author(s):  
Ekaterina V. Filippova ◽  
Zdzislaw Wawrzak ◽  
Jiapeng Ruan ◽  
Sergii Pshenychnyi ◽  
Richard M. Schultz ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Stress Response ◽  
Response Regulator ◽  
Fromescherichia Coli ◽  
Receiver Domain

scholarly journals Crystal Structure of the CheA Histidine Phosphotransfer Domain that Mediates Response Regulator Phosphorylation in Bacterial Chemotaxis

2001 ◽  
Vol 276 (33) ◽  
pp. 31074-31082 ◽  
Author(s):  
Lionel Mourey ◽  
Sandra Da Re ◽  
Jean-Denis Pédelacq ◽  
Tatiana Tolstykh ◽  
Cécile Faurie ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Response Regulator ◽  
Bacterial Chemotaxis ◽  
Histidine Phosphotransfer

scholarly journals Crystal structure of an α/β serine hydrolase (YDR428C) from Saccharomyces cerevisiae at 1.85 Å resolution

2004 ◽  
Vol 58 (3) ◽  
pp. 755-758 ◽  
Author(s):  
Joseph W. Arndt ◽  
Robert Schwarzenbacher ◽  
Rebecca Page ◽  
Polat Abdubek ◽  
Eileen Ambing ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Saccharomyces Cerevisiae ◽  
Serine Hydrolase

scholarly journals The crystal structure of microtubule-associated protein light chain 3, a mammalian homologue of Saccharomyces cerevisiae Atg8

2004 ◽  
Vol 9 (7) ◽  
pp. 611-618 ◽  
Author(s):  
Kenji Sugawara ◽  
Nobuo N. Suzuki ◽  
Yuko Fujioka ◽  
Noboru Mizushima ◽  
Yoshinori Ohsumi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Saccharomyces Cerevisiae ◽  
Light Chain ◽  
Mammalian Homologue

scholarly journals The crystal structure and identification of NQM1/YGR043C, a transaldolase from Saccharomyces cerevisiae

2008 ◽  
Vol 73 (4) ◽  
pp. 1076-1081 ◽  
Author(s):  
Hua Huang ◽  
Hui Rong ◽  
Xu Li ◽  
Shuilong Tong ◽  
Zhiqiang Zhu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Saccharomyces Cerevisiae

Peroxisomal multifunctional enzyme type 2 from the fruitfly: dehydrogenase and hydratase act as separate entities, as revealed by structure and kinetics

2011 ◽  
Vol 435 (3) ◽  
pp. 771-781 ◽  
Author(s):  
Tatu J. K. Haataja ◽  
M. Kristian Koski ◽  
J. Kalervo Hiltunen ◽  
Tuomo Glumoff
Keyword(s):  
Crystal Structure ◽  
Saccharomyces Cerevisiae ◽  
Drosophila Melanogaster ◽  
Structural Features ◽  
Full Length ◽  
Multifunctional Enzyme ◽  
Domain Composition ◽  
Substrate Channelling

All of the peroxisomal β-oxidation pathways characterized thus far house at least one MFE (multifunctional enzyme) catalysing two out of four reactions of the spiral. MFE type 2 proteins from various species display great variation in domain composition and predicted substrate preference. The gene CG3415 encodes for Drosophila melanogaster MFE-2 (DmMFE-2), complements the Saccharomyces cerevisiae MFE-2 deletion strain, and the recombinant protein displays both MFE-2 enzymatic activities in vitro. The resolved crystal structure is the first one for a full-length MFE-2 revealing the assembly of domains, and the data can also be transferred to structure–function studies for other MFE-2 proteins. The structure explains the necessity of dimerization. The lack of substrate channelling is proposed based on both the structural features, as well as by the fact that hydration and dehydrogenation activities of MFE-2, if produced as separate enzymes, are equally efficient in catalysis as the full-length MFE-2.

scholarly journals THE APPLICABILITY OF THE CRYSTAL STRUCTURE OF TERMOTOGA MARITIMA 4--GLUCANOTRANSFERASE AS THE TEMPLATE FOR SULOCHRIN AS -GLUCOSIDASE INHIBITORS

2010 ◽  
Vol 9 (3) ◽  
pp. 479-486
Author(s):  
Rizna Triana Dewi ◽  
Yulia Anita ◽  
Enade Perdana Istyastono ◽  
Akhmad Darmawan ◽  
Muhamad Hanafi
Keyword(s):  
Crystal Structure ◽  
Saccharomyces Cerevisiae ◽  
Thermotoga Maritima ◽  
Binding Pocket ◽  
Operating Environment ◽  
High Sequence Identity ◽  
Glucosidase Inhibitor ◽  
Glucosidase Inhibitors ◽  
Docking Method ◽  
Binding Residues

Interaction of sulochrin to active site of glucosidase enzyme of Termotoga maritime has been studied by employing docking method using Molecular Operating Environment (MOE), in comparison with those are reports of established inhibitor α-glucosidase such as acarbose, miglitol and voglibose, and salicinol, as reference compounds. The crystal structure T. maritima α-glucanotransferase (PDB code: 1LWJ) can be employed to serve as the template in the virtual screening of S. cerevisiae α-glucosidase. The comparison between the binding pocket residues of Thermotoga maritima α-glucanotransferase and Saccharomyces cerevisiae α-glucosidase show a high sequence identity and similarity. The result showed that sulochrin could be located in the binding pocket and formed some interactions with the binding residues. The ligands showed proper predicted binding energy (-6.74 - -4.13 kcal/mol) and predicted Ki values (0.011 - 0.939 mM). Sulochrin has a possibility to serve as a lead compound in the development of new α-glucosidase inhibitor.   Keywords: Docking, sulochrin, α-glucosidase Inhibitor, Thermotoga maritime α-glucotransferase, Saccharomyces cerevisiae α-glucosidase, MOE

Sign in / Sign up

Export Citation Format

Share Document