Results 31 to 40 of about 574,974 (306)

Essential role of the C-terminal helical domain in active site formation of selenoprotein MsrA from Clostridium oremlandii. [PDF]

open access: yesPLoS ONE, 2015
We previously determined the crystal structures of 1-Cys type selenoprotein MsrA from Clostridium oremlandii (CoMsrA). The overall structure of CoMsrA is unusual, consisting of two domains, the N-terminal catalytic domain and the C-terminal distinct ...
Eun Hye Lee   +3 more
doaj   +1 more source

Structure- and context-based analysis of the GxGYxYP family reveals a new putative class of glycoside hydrolase. [PDF]

open access: yes, 2014
BackgroundGut microbiome metagenomics has revealed many protein families and domains found largely or exclusively in that environment. Proteins containing the GxGYxYP domain are over-represented in the gut microbiota, and are found in Polysaccharide ...
Chang, Yuanyuan   +5 more
core   +2 more sources

The chitinase C gene PsChiC from Pseudomonas sp. and its synergistic effects on larvicidal activity

open access: yesGenetics and Molecular Biology, 2015
Pseudomonas sp. strain TXG6-1, a chitinolytic gram-negative bacterium, was isolated from a vegetable field in Taixing city, Jiangsu Province, China. In this study, a Pseudomonas chitinase C gene (PsChiC) was isolated from the chromosomal DNA of this ...
Wanfang Zhong, Shaojun Ding, Huifang Guo
doaj   +1 more source

Structure of Mycobacterium tuberculosis Cya, an evolutionary ancestor of the mammalian membrane adenylyl cyclases

open access: yeseLife, 2022
Mycobacterium tuberculosis adenylyl cyclase (AC) Rv1625c/Cya is an evolutionary ancestor of the mammalian membrane ACs and a model system for studies of their structure and function.
Ved Mehta   +9 more
doaj   +1 more source

Structure, function and inhibition of poly(ADP-ribose)polymerase, member 14 (PARP14) [PDF]

open access: yes, 2018
Poly(ADP-ribose)polymerase, member 14 (PARP14, alternatively named ARTD8, BAL2, and COAST6) is an intracellular mono(ADP-ribosyl) transferase. PARP14 transfers a negatively charged ADP-ribose unit from a donor NAD+ molecule onto a target protein, post ...
Levonis, Stephan M   +3 more
core   +1 more source

RBR E3 ubiquitin ligases: new structures, new insights, new questions [PDF]

open access: yes, 2014
The RBR (RING-BetweenRING-RING) or TRIAD [two RING fingers and a DRIL (double RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex multidomain enzymes.
Shaw, Gary S.   +2 more
core   +1 more source

Two Catalytic Domains Are Required for Protein Deacetylation [PDF]

open access: yesJournal of Biological Chemistry, 2006
Histone deacetylase (HDAC)-6 was recently identified as a dual substrate, possibly multisubstrate, deacetylase that can act both on acetylated histone tails and on alpha-tubulin acetylated on Lys40. HDAC-6 is unique among deacetylases in having two hdac domains, and we have used this enzyme as a useful model to dissect the structural requirements for ...
Zhang, Yu   +3 more
openaire   +3 more sources

Phosphorylated claspin interacts with a phosphate-binding site in the kinase domain of Chk1 during ATR-mediated activation [PDF]

open access: yes, 2003
Claspin is essential for the ATR-dependent activation of Chk1 in Xenopus egg extracts containing incompletely replicated or UV-damaged DNA. The activated form of Claspin contains two repeated phosphopeptide motifs that mediate its binding to Chk1.
Dunphy, William G.   +3 more
core   +1 more source

Structural rearrangement of CaMKIIα catalytic domains encodes activation [PDF]

open access: yesProceedings of the National Academy of Sciences, 2009
At its fundamental level, human memory is thought to occur at individual synaptic contact sites and manifest as persistent changes in synaptic efficacy. In digital electronics, the fundamental structure for implementing memory is the flip-flop switch, a circuit that can be triggered to flip between two stable states.
Christopher, Thaler   +4 more
openaire   +2 more sources

Allosteric Regulation Alters Carrier Domain Translocation in Pyruvate Carboxylase [PDF]

open access: yes, 2018
Pyruvate carboxylase (PC) catalyzes the ATP-dependent carboxylation of pyruvate to oxaloacetate. The reaction occurs in two separate catalytic domains, coupled by the long-range translocation of a biotinylated carrier domain (BCCP). Here, we use a series
Budelier, Melissa M.   +3 more
core   +3 more sources

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