ATP-binding motifs

Adenosine 5'-triphosphate (ATP) binds to a great number of proteins to elicit a wide variety of effects, including energy production and molecular signalling. Proteins have evolved different strategies to specifically recognize ATP, utilizing different ways of binding the phosphoryl moieties as well as the adenine base. The most common, conserved sequence and structural motif for binding ATP is the Walker-A motif, or P-loop, found in many different protein structural families. Greater variation in the sequence of the P-loop is being recognized, as more ATP-binding proteins are being structurally and functionally characterized. In contrast to the P-loop, recognition of the adenine base often makes use of conserved structural motifs of main-chain atoms via hydrogen-bonding interactions, or side-chains in stacking interactions, without a definitive amino acid sequence pattern.Peer reviewed: YesNRC publication: Ye

Crystallization and preliminary X-ray studies of the N-domain of the Wilson disease associated protein

The modified N-domain of the Wilson disease protein has been crystallized both in its native form and as a selenomethionine derivative. X-ray diffraction data were collected from the native crystal to 1.7 Å resolution, while the selenomethionine derivative diffracted to 2.7 Å resolution

Crystallization, preliminary X-ray diffraction and structure analysis of Thermotoga maritima mannitol dehydrogenase

T. maritima mannitol dehydrogenase has been crystallized in space group P212121 with a = 84.43, b = 120.61, c = 145.76 Å. The crystals diffracted to 3.3 Å resolution at the Canadian Light Source

Crystallization, preliminary X-ray diffraction and structure solution of MosA, a dihydrodipicolinate synthase from Sinorhizobium meliloti L5-30

MosA from S. meliloti L5-30 has been crystallized in solution with pyruvate and the 2.3 Å resolution structure has been solved by molecular replacement using E. coli dihydrodipicolinate synthase as the model

Crystallization and preliminary X-ray diffraction analysis of the Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase I86A mutant

The secondary alcohol dehydrogenase mutant I86A from Thermoanaerobacter ethanolicus (TeSADH) was crystallized in novel crystallization conditions. Diffraction data to 3.2 Å were collected at the Canadian Light Source