Characterization of a Membrane‐Bound O ‐Acetyltransferase Involved in Trioxacarcin Biosynthesis Offers Insights into Its Catalytic Mechanism †

2020 ◽  
Vol 38 (12) ◽  
pp. 1607-1611
Author(s):  
Yue Yin ◽  
Yi Shen ◽  
Song Meng ◽  
Mei Zhang ◽  
Hai‐Xue Pan ◽  
...  
Keyword(s):  
Catalytic Mechanism ◽  
Membrane Bound

Structural and biochemical characterization of the catalytic domains of GdpP reveals a unified hydrolysis mechanism for the DHH/DHHA1 phosphodiesterase

2018 ◽  
Vol 475 (1) ◽  
pp. 191-205 ◽  
Author(s):  
Feng Wang ◽  
Qing He ◽  
Kaixuan Su ◽  
Tiandi Wei ◽  
Sujuan Xu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Catalytic Mechanism ◽  
Biochemical Characterization ◽  
Adenosine Monophosphate ◽  
Guanosine Monophosphate ◽  
Catalytic Domains ◽  
Membrane Bound ◽  
Nucleotide Specificity ◽  
Binding Position

The Asp-His-His and Asp-His-His-associated (DHH/DHHA1) domain-containing phosphodiesterases (PDEs) that catalyze degradation of cyclic di-adenosine monophosphate (c-di-AMP) could be subdivided into two subfamilies based on the final product [5′-phosphadenylyl-adenosine (5′-pApA) or AMP]. In a previous study, we revealed that Rv2837c, a stand-alone DHH/DHHA1 PDE, employs a 5′-pApA internal flipping mechanism to produce AMPs. However, why the membrane-bound DHH/DHHA1 PDE can only degrade c-di-AMP to 5′-pApA remains obscure. Here, we report the crystal structure of the DHH/DHHA1 domain of GdpP (GdpP-C), and structures in complex with c-di-AMP, cyclic di-guanosine monophosphate (c-di-GMP), and 5′-pApA. Structural analysis reveals that GdpP-C binds nucleotide substrates quite differently from how Rv2837c does in terms of substrate-binding position. Accordingly, the nucleotide-binding site of the DHH/DHHA1 PDEs is organized into three (C, G, and R) subsites. For GdpP-C, in the C and G sites c-di-AMP binds and degrades into 5′-pApA, and its G site determines nucleotide specificity. To further degrade into AMPs, 5′-pApA must slide into the C and R sites for flipping and hydrolysis as in Rv2837c. Subsequent mutagenesis and enzymatic studies of GdpP-C and Rv2837c uncover the complete flipping process and reveal a unified catalytic mechanism for members of both DHH/DHHA1 PDE subfamilies.

scholarly journals Isolation and characterization of a membrane protein from rat erythrocytes which inhibits lysis by the membrane attack complex of rat complement

1992 ◽  
Vol 284 (1) ◽  
pp. 169-176 ◽  
Author(s):  
T R Hughes ◽  
S J Piddlesden ◽  
J D Williams ◽  
R A Harrison ◽  
B P Morgan
Keyword(s):  
Affinity Purification ◽  
Membrane Attack Complex ◽  
Erythrocyte Membranes ◽  
Dependent Manner ◽  
Inhibitory Protein ◽  
Rat Erythrocytes ◽  
Butanol Extract ◽  
Isolation And Characterization ◽  
Membrane Bound

The membrane attack complex (MAC) of complement in humans is regulated by several membrane-bound proteins; however, no such proteins have so far been described in other species. Here we report the isolation and characterization of a rat erythrocyte membrane glycoprotein of molecular mass 21 kDa which inserts into cell membranes and is a potent inhibitor of the rat MAC. This protein, here called rat inhibitory protein (RIP), was first partially purified by column chromatography from a butanol extract of rat erythrocyte membranes. Monoclonal antibodies (Mabs) were raised against RIP and used for its affinity purification. Affinity-purified RIP was shown to inhibit in a dose-dependent manner the cobra venom factor (CVF)-mediated ‘reactive’ lysis of guinea pig erythrocytes by rat complement. Conversely, the anti-RIP MAbs 6D1 and TH9 were shown to markedly enhance the CVF-mediated lysis of rat erythrocytes by rat complement. RIP acted late in the assembly of the MAC (at or after the C5b-8 stage) and was releasable from the membranes of rat erythrocytes by phosphatidylinositol-specific phospholipase C. These features, together with its size, deglycosylation pattern and N-terminal amino acid sequence, lead us to conclude that RIP is the rat homologue of the human MAC-inhibitory protein CD59 antigen.

Characterization of soluble vs membrane-bound human placental 5′-nucleotidase

1990 ◽  
Vol 172 (3) ◽  
pp. 1371-1377 ◽  
Author(s):  
Mary R. Klemens ◽  
William R. Sherman ◽  
Nels J. Holmberg ◽  
Julie M. Ruedi ◽  
Martin G. Low ◽  
...  
Keyword(s):  
Membrane Bound

scholarly journals Characterization of Nicotinamidases: Steady State Kinetic Parameters, Classwide Inhibition by Nicotinaldehydes, and Catalytic Mechanism

Biochemistry ◽  
2010 ◽  
Vol 49 (49) ◽  
pp. 10421-10439 ◽  
Author(s):  
Jarrod B. French ◽  
Yana Cen ◽  
Tracy L. Vrablik ◽  
Ping Xu ◽  
Eleanor Allen ◽  
...  
Keyword(s):  
Steady State ◽  
Kinetic Parameters ◽  
Catalytic Mechanism ◽  
Steady State Kinetic ◽  
State Kinetic

scholarly journals Structural characterization of membrane-bound human immunodeficiency virus-1 Gag matrix with neutron reflectometry

2017 ◽  
Vol 12 (2) ◽  
pp. 02D408 ◽  
Author(s):  
Rebecca Eells ◽  
Marilia Barros ◽  
Kerry M. Scott ◽  
Ioannis Karageorgos ◽  
Frank Heinrich ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Structural Characterization ◽  
Neutron Reflectometry ◽  
Immunodeficiency Virus ◽  
Membrane Bound ◽  
Human Immunodeficiency Virus 1

Detection and Characterization of Membrane-Bound Selenoproteins in the Kidney of the Rat

2002 ◽  
Vol 973 (1) ◽  
pp. 289-292 ◽  
Author(s):  
A. KYRIAKOPOULOS ◽  
H. BERTELSMANN ◽  
A. GRAEBERT ◽  
B. HOPPE ◽  
M. KÜHBACHER ◽  
...  
Keyword(s):  
Membrane Bound
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