Crystal Structure of Homoserine Transacetylase fromHaemophilus influenzaeReveals a New Family of α/β-Hydrolases†,‡

Biochemistry ◽  
2005 ◽  
Vol 44 (48) ◽  
pp. 15768-15773 ◽  
Author(s):  
I. Ahmad Mirza ◽  
Ishac Nazi ◽  
Magdalena Korczynska ◽  
Gerard D. Wright ◽  
Albert M. Berghuis
Keyword(s):  
Crystal Structure ◽  
New Family ◽  
Homoserine Transacetylase

Crystal Structure of Bordetella pertussis BugD Solute Receptor Unveils the Basis of Ligand Binding in a New Family of Periplasmic Binding Proteins

2006 ◽  
Vol 356 (4) ◽  
pp. 1014-1026 ◽  
Author(s):  
Isabelle Huvent ◽  
Hassan Belrhali ◽  
Rudy Antoine ◽  
Coralie Bompard ◽  
Camille Locht ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ligand Binding ◽  
Bordetella Pertussis ◽  
Binding Proteins ◽  
New Family ◽  
Periplasmic Binding Proteins

A novel hexanuclear titanium(iv)-oxo-iminodiacetate cluster with a Ti6O9 core: single-crystal structure and photocatalytic activities

2016 ◽  
Vol 45 (18) ◽  
pp. 7581-7588 ◽  
Author(s):  
Lubin Ni ◽  
Dashuai Liang ◽  
Yin Cai ◽  
Guowang Diao ◽  
Zhaohui Zhou
Keyword(s):  
Crystal Structure ◽  
Visible Light ◽  
Single Crystal ◽  
Single Crystal Structure ◽  
New Family ◽  
Photocatalytic Activities

A new family of hexanuclear titanium(iv)-oxo-carboxylate cluster containing a {Ti6O9} core exhibiting remarkable potential as a visible-light homogeneous photocatalyst.

A New Family of Lithium Rare-Earth Oxyborates, LiLn6O5(BO3)3 (Ln=Pr–Tm): Crystal Structure of the Gadolinium Phase LiGd6O5(BO3)3

1999 ◽  
Vol 146 (1) ◽  
pp. 189-196 ◽  
Author(s):  
Jean-Pierre Chaminade ◽  
Pierre Gravereau ◽  
Veronique Jubera ◽  
Claude Fouassier
Keyword(s):  
Crystal Structure ◽  
Rare Earth ◽  
New Family

Aloisines, a New Family of CDK/GSK-3 Inhibitors. SAR Study, Crystal Structure in Complex with CDK2, Enzyme Selectivity, and Cellular Effects

2003 ◽  
Vol 46 (2) ◽  
pp. 222-236 ◽  
Author(s):  
Yvette Mettey ◽  
Marie Gompel ◽  
Virginie Thomas ◽  
Matthieu Garnier ◽  
Maryse Leost ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Cellular Effects ◽  
New Family ◽  
Sar Study ◽  
Enzyme Selectivity

Simple Synthesis of New Mixed Isocyanide-NHC-Platinum(II) Complexes and Their Catalytic Activity

2014 ◽  
Vol 67 (3) ◽  
pp. 469 ◽  
Author(s):  
Christoph Hubbert ◽  
Marcus Breunig ◽  
Kristen J. Carroll ◽  
Frank Rominger ◽  
A. Stephen K. Hashmi
Keyword(s):  
Crystal Structure ◽  
Catalytic Activity ◽  
Structural Data ◽  
Simple Synthesis ◽  
X Ray ◽  
New Family ◽  
Catalytically Active ◽  
Convergent Approach ◽  
New Compounds

Using the new modular and convergent approach to isocyanide-N-hetrocyclic carbene-platinum(ii) complexes, eight new compounds have been synthesised. For three of these, detailed structural data could be obtained by X-ray crystal structure analyses. This new family of organoplatinum complexes is catalytically active for hydrosilylation reactions; styrene and phenylacetylene could be used as substrates; triethylsilane and 1,1,1,3,5,5,5-heptamethyltrisiloxane could be used as reagents. With some of the new platinum pre-catalysts, excellent regioselectivities of up to 98 : 2 could be obtained, and turnover numbers up to 840 were achieved.

scholarly journals The Crystal Structure of Rv0813c from Mycobacterium tuberculosis Reveals a New Family of Fatty Acid-Binding Protein-Like Proteins in Bacteria

2006 ◽  
Vol 189 (5) ◽  
pp. 1899-1904 ◽  
Author(s):  
William Shepard ◽  
Ahmed Haouz ◽  
Martin Graña ◽  
Alejandro Buschiazzo ◽  
Jean-Michel Betton ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Mycobacterium Tuberculosis ◽  
Fatty Acid ◽  
Double Helix ◽  
Internal Surface ◽  
Hypothetical Protein ◽  
Hydroxyl Group ◽  
Fatty Acid Binding Proteins ◽  
Fatty Acid Binding ◽  
New Family

ABSTRACT The gene Rv0813c from Mycobacterium tuberculosis, which codes for a hypothetical protein of unknown function, is conserved within the order Actinomycetales but absent elsewhere. The crystal structure of Rv0813c reveals a new family of proteins that resemble the fatty acid-binding proteins (FABPs) found in eukaryotes. Rv0813c adopts the 10-stranded β-barrel fold typical of FABPs but lacks the double-helix insert that covers the entry to the binding site in the eukaryotic proteins. The barrel encloses a deep cavity, at the bottom of which a small cyclic ligand was found to bind to the hydroxyl group of Tyr192. This residue is part of a conserved Arg-X-Tyr motif much like the triad that binds the carboxylate group of fatty acids in FABPs. Most of the residues forming the internal surface of the cavity are conserved in homologous protein sequences found in CG-rich prokaryotes, strongly suggesting that Rv0813c is a member of a new family of bacterial FABP-like proteins that may have roles in the recognition, transport, and/or storage of small molecules in the bacterial cytosol.

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