Crystal Structure and Functional Assignment of YfaU, a Metal Ion Dependent Class II Aldolase fromEscherichia coliK12†‡

Biochemistry ◽  
2008 ◽  
Vol 47 (38) ◽  
pp. 9955-9965 ◽  
Author(s):  
Dean Rea ◽  
Rebecca Hovington ◽  
John F. Rakus ◽  
John A. Gerlt ◽  
Vilmos Fülöp ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Metal Ion ◽  
Class Ii ◽  
Functional Assignment ◽  
Class Ii Aldolase

scholarly journals Crystal Structure of Reaction Intermediates in Pyruvate Class II Aldolase

2012 ◽  
Vol 287 (43) ◽  
pp. 36208-36221 ◽  
Author(s):  
Mathieu Coincon ◽  
Weijun Wang ◽  
Jurgen Sygusch ◽  
Stephen Y. K. Seah
Keyword(s):  
Crystal Structure ◽  
Class Ii ◽  
Reaction Intermediates ◽  
Class Ii Aldolase

scholarly journals Metal ion influences distortion of the ligand in the structure of [M{2-MeO(O)CC6H4NHC(S)NP(S)(OiPr)2}2] (M = ZnII, CdII) complexes: a driving force for intermolecular aggregation

2015 ◽  
Vol 44 (31) ◽  
pp. 14101-14109 ◽  
Author(s):  
Damir A. Safin ◽  
Maria G. Babashkina ◽  
Michael Bolte ◽  
Mariusz P. Mitoraj ◽  
Axel Klein
Keyword(s):  
Crystal Structure ◽  
Metal Cation ◽  
Driving Force ◽  
Metal Ion ◽  
Supramolecular Aggregation

Reaction of the deprotonated 2-MeO(O)CC6H4NHC(S)NHP(S)(OiPr)2 (HL) with ZnII or CdII leads to [ZnL2] and [CdL2]. The nature of the metal cation (ZnIIvs. CdII) drives the supramolecular aggregation of molecules in the crystal structure.

The crystal structure of staphylococcal enterotoxin H: implications for binding properties to MHC class II and TcR molecules

2000 ◽  
Vol 302 (3) ◽  
pp. 527-537 ◽  
Author(s):  
M Håkansson ◽  
K Petersson ◽  
H Nilsson ◽  
G Forsberg ◽  
P Björk ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Mhc Class Ii ◽  
Class Ii ◽  
Staphylococcal Enterotoxin ◽  
Binding Properties

scholarly journals How cyanophage S-2L rejects adenine and incorporates 2-aminoadenine to saturate hydrogen bonding in its DNA

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Dariusz Czernecki ◽  
Pierre Legrand ◽  
Mustafa Tekpinar ◽  
Sandrine Rosario ◽  
Pierre-Alexandre Kaminski ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Hydrogen Bonding ◽  
Crystal Structures ◽  
Active Site ◽  
Metal Ion ◽  
Restriction Endonucleases ◽  
Structural Element

AbstractBacteriophages have long been known to use modified bases in their DNA to prevent cleavage by the host’s restriction endonucleases. Among them, cyanophage S-2L is unique because its genome has all its adenines (A) systematically replaced by 2-aminoadenines (Z). Here, we identify a member of the PrimPol family as the sole possible polymerase of S-2L and we find it can incorporate both A and Z in front of a T. Its crystal structure at 1.5 Å resolution confirms that there is no structural element in the active site that could lead to the rejection of A in front of T. To resolve this contradiction, we show that a nearby gene is a triphosphohydolase specific of dATP (DatZ), that leaves intact all other dNTPs, including dZTP. This explains the absence of A in S-2L genome. Crystal structures of DatZ with various ligands, including one at sub-angstrom resolution, allow to describe its mechanism as a typical two-metal-ion mechanism and to set the stage for its engineering.

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