Structural Basis of Allosteric Regulation and Substrate Specificity of the Non-Phosphorylating Glyceraldehyde 3-Phosphate Dehydrogenase from Thermoproteus tenax

2004 ◽  
Vol 341 (3) ◽  
pp. 815-828 ◽  
Author(s):  
Esben Lorentzen ◽  
Reinhard Hensel ◽  
Thomas Knura ◽  
Hatim Ahmed ◽  
Ehmke Pohl
Keyword(s):  
Substrate Specificity ◽  
Allosteric Regulation ◽  
Structural Basis ◽  
Thermoproteus Tenax

scholarly journals Correction: Dynamic properties of dipeptidyl peptidase III from Bacteroides thetaiotaomicron and the structural basis for its substrate specificity – a computational study

2017 ◽  
Vol 13 (12) ◽  
pp. 2729-2730
Author(s):  
M. Tomin ◽  
S. Tomić
Keyword(s):  
Substrate Specificity ◽  
Computational Study ◽  
Dynamic Properties ◽  
Dipeptidyl Peptidase ◽  
Structural Basis ◽  
Bacteroides Thetaiotaomicron

Correction for ‘Dynamic properties of dipeptidyl peptidase III from Bacteroides thetaiotaomicron and the structural basis for its substrate specificity – a computational study’ by M. Tomin et al., Mol. BioSyst., 2017, 13, 2407–2417.

Structural insights into the substrate specificity of a glycoside hydrolase family 5 lichenase from Caldicellulosiruptor sp. F32

2017 ◽  
Vol 474 (20) ◽  
pp. 3373-3389 ◽  
Author(s):  
Dong-Dong Meng ◽  
Xi Liu ◽  
Sheng Dong ◽  
Ye-Fei Wang ◽  
Xiao-Qing Ma ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Substrate Specificity ◽  
Glycoside Hydrolase ◽  
Complex Structure ◽  
Dynamics Simulation ◽  
Structural Basis ◽  
Glycoside Hydrolase Family ◽  
Substrate Selectivity ◽  
Glucose Residue ◽  
Structural Insights

Glycoside hydrolase (GH) family 5 is one of the largest GH families with various GH activities including lichenase, but the structural basis of the GH5 lichenase activity is still unknown. A novel thermostable lichenase F32EG5 belonging to GH5 was identified from an extremely thermophilic bacterium Caldicellulosiruptor sp. F32. F32EG5 is a bi-functional cellulose and a lichenan-degrading enzyme, and exhibited a high activity on β-1,3-1,4-glucan but side activity on cellulose. Thin-layer chromatography and NMR analyses indicated that F32EG5 cleaved the β-1,4 linkage or the β-1,3 linkage while a 4-O-substitued glucose residue linked to a glucose residue through a β-1,3 linkage, which is completely different from extensively studied GH16 lichenase that catalyses strict endo-hydrolysis of the β-1,4-glycosidic linkage adjacent to a 3-O-substitued glucose residue in the mixed-linked β-glucans. The crystal structure of F32EG5 was determined to 2.8 Å resolution, and the crystal structure of the complex of F32EG5 E193Q mutant and cellotetraose was determined to 1.7 Å resolution, which revealed that the exit subsites of substrate-binding sites contribute to both thermostability and substrate specificity of F32EG5. The sugar chain showed a sharp bend in the complex structure, suggesting that a substrate cleft fitting to the bent sugar chains in lichenan is a common feature of GH5 lichenases. The mechanism of thermostability and substrate selectivity of F32EG5 was further demonstrated by molecular dynamics simulation and site-directed mutagenesis. These results provide biochemical and structural insights into thermostability and substrate selectivity of GH5 lichenases, which have potential in industrial processes.

βD305A Mutant of Tryptophan Synthase Shows Strongly Perturbed Allosteric Regulation and Substrate Specificity†

Biochemistry ◽  
2001 ◽  
Vol 40 (25) ◽  
pp. 7421-7432 ◽  
Author(s):  
Davide Ferrari ◽  
Li-Hong Yang ◽  
Edith W. Miles ◽  
Michael F. Dunn
Keyword(s):  
Substrate Specificity ◽  
Allosteric Regulation ◽  
Tryptophan Synthase

scholarly journals Structural Basis for Substrate Specificity ofEscherichia coliPurine Nucleoside Phosphorylase

2003 ◽  
Vol 278 (47) ◽  
pp. 47110-47118 ◽  
Author(s):  
Eric M. Bennett ◽  
Chenglong Li ◽  
Paula W. Allan ◽  
William B. Parker ◽  
Steven E. Ealick
Keyword(s):  
Substrate Specificity ◽  
Structural Basis ◽  
Nucleoside Phosphorylase

scholarly journals Structural basis for catalysis and substrate specificity of human ACAT1

Nature ◽  
2020 ◽  
Vol 581 (7808) ◽  
pp. 333-338 ◽  
Author(s):  
Hongwu Qian ◽  
Xin Zhao ◽  
Renhong Yan ◽  
Xia Yao ◽  
Shuai Gao ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Structural Basis

Structural Basis of Substrate Specificity of Plant 12-Oxophytodienoate Reductases

2009 ◽  
Vol 392 (5) ◽  
pp. 1266-1277 ◽  
Author(s):  
Constanze Breithaupt ◽  
Robert Kurzbauer ◽  
Florian Schaller ◽  
Annick Stintzi ◽  
Andreas Schaller ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Structural Basis

Structural basis for the allosteric regulation of the SbtA bicarbonate transporter by the PII-like protein, SbtB, from Cyanobium sp. PCC7001

2019 ◽  
Author(s):  
Joe A. Kaczmarski ◽  
Nan-Sook Hong ◽  
Bratati Mukherjee ◽  
Laura T. Wey ◽  
Loraine Rourke ◽  
...  
Keyword(s):  
Metal Ion ◽  
Transcriptional Control ◽  
Allosteric Regulation ◽  
Inhibitory Effect ◽  
Photosynthetic Performance ◽  
Regulatory Proteins ◽  
Structural Basis ◽  
Titration Calorimetry ◽  
X Ray ◽  
Bicarbonate Transporter

ABSTRACTCyanobacteria have evolved a suite of enzymes and inorganic carbon (Ci) transporters that improve photosynthetic performance by increasing the localized concentration of CO2 around the primary CO2-fixating enzyme, Rubisco. This CO2-concentrating mechanism (CCM) is highly regulated, responds to illumination/darkness cycles and allows cyanobacteria to thrive under limiting Ci conditions. While the transcriptional control of CCM activity is well understood, less is known about how regulatory proteins might allosterically regulate Ci transporters in response to changing conditions. Cyanobacterial sodium-dependent bicarbonate transporters (SbtAs) are inhibited by PII-like regulatory proteins (SbtBs), with the inhibitory effect being modulated by adenylnucleotides. Here, we used isothermal titration calorimetry to show that SbtB from Cyanobium sp. PCC7001 (SbtB7001) binds AMP, ADP, cAMP and ATP with micromolar-range affinities. X-ray crystal structures of apo- and nucleotide-bound SbtB7001 revealed that while AMP, ADP and cAMP have little effect on the SbtB7001 structure, binding of ATP stabilizes the otherwise flexible T-loop and that the flexible C-terminal C-loop adopts several distinct conformations. We also show that ATP binding affinity is increased ten-fold in the presence of Ca2+ and we present an X-ray crystal structure of Ca2+ATP:SbtB7001 that shows how this metal ion facilitates additional stabilizing interactions with the apex of the T-loop. We propose that the Ca2+ATP-induced conformational change observed in SbtB7001 is important for allosteric regulation of SbtA activity by SbtB and is consistent with changing adenylnucleotide levels in illumination/darkness cycles.GRAPHICAL ABSTRACT

Structural Basis for Substrate Specificity and Carbapenemase Activity of OXA-48 Class D β-Lactamase

2019 ◽  
Vol 6 (2) ◽  
pp. 261-271 ◽  
Author(s):  
Afroza Akhtar ◽  
Orville A. Pemberton ◽  
Yu Chen
Keyword(s):  
Substrate Specificity ◽  
Structural Basis ◽  
Class D
Sign in / Sign up

Export Citation Format

Share Document