Výsledky vyhledávání

Crystal structure of a protein repair methyltransferase from Pyrococcus furiosus with its L-isoaspartyl peptide substrate

Autor: S C, Griffith, M R, Sawaya, D R, Boutz, N, Thapar, J E, Katz, S, Clarke, T O, Yeates

Publikováno v: Journal of molecular biology. 313(5)

Protein L-isoaspartyl (D-aspartyl) methyltransferases (EC 2.1.1.77) are found in almost all organisms. These enzymes catalyze the S-adenosylmethionine (AdoMet)-dependent methylation of isomerized and racemized aspartyl residues in age-damaged protein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::455d880d8f7a812bfeee650ac0775017
https://pubmed.ncbi.nlm.nih.gov/11700066

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The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds

Autor: E A, Toth, C, Worby, J E, Dixon, E R, Goedken, S, Marqusee, T O, Yeates

Publikováno v: Journal of molecular biology. 301(2)

Adenylosuccinate lyase catalyzes two separate reactions in the de novo purine biosynthetic pathway. Through its dual action in this pathway, adenylosuccinate lyase plays an integral part in cellular replication and metabolism. Mutations in the human

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4266189ff07eeeea33f19fcd739ce572
https://pubmed.ncbi.nlm.nih.gov/10926519

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Searching for frameshift evolutionary relationships between protein sequence families

Autor: M, Pellegrini, T O, Yeates

Publikováno v: Proteins. 37(2)

The protein sequence database was analyzed for evidence that some distinct sequence families might be distantly related in evolution by changes in frame of translation. Sequences were compared using special amino acid substitution matrices for the al

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::95111bafd3646654d0b2d631182b6395
https://pubmed.ncbi.nlm.nih.gov/10584072

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A fast algorithm for genome-wide analysis of proteins with repeated sequences

Autor: M, Pellegrini, E M, Marcotte, T O, Yeates

Publikováno v: Proteins. 35(4)

We present a fast algorithm to search for repeating fragments within protein sequences. The technique is based on an extension of the Smith-Waterman algorithm that allows the calculation of sub-optimal alignments of a sequence against itself. We are

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c5ab0861dbbc9fbf069f97b46671640d
https://pubmed.ncbi.nlm.nih.gov/10382671

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Highly constrained multiple-copy refinement of protein crystal structures

Autor: M, Pellegrini, N, Grønbech-Jensen, J A, Kelly, G M, Pfluegl, T O, Yeates

Publikováno v: Proteins. 29(4)

In the course of refining atomic protein structures, one often encounters difficulty with molecules that are unusually flexible or otherwise disordered. We approach the problem by combining two relatively recent developments: simultaneous refinement

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::dcbf2bae84527673317368a6e8358b28
https://pubmed.ncbi.nlm.nih.gov/9408940

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Simulation of protein crystal nucleation

Autor: M, Pellegrini, S W, Wukovitz, T O, Yeates

Publikováno v: Proteins. 28(4)

To attempt to understand the physical principles underlying protein crystallization, an algorithm is described for simulating the crystal nucleation event computationally. The validity of the approach is supported by its ability to reproduce closely

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5af2995a4667dd38218234596f808b64
https://pubmed.ncbi.nlm.nih.gov/9261867

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Detecting and overcoming crystal twinning

Autor: T O, Yeates

Publikováno v: Methods in enzymology. 276

Twinning is fairly common in protein crystals. In its merohedral from, twinning is not apparent in the diffraction pattern, but the observed intensities do not represent individual crystallographic intensities. Since partial twinning (twin fraction l

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::39a86b7412793e077fc8da9e5ce271c4
https://pubmed.ncbi.nlm.nih.gov/9048378

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Crystallization and preliminary structural analysis of Bacillus subtilis adenylosuccinate lyase, an enzyme implicated in infantile autism

Autor: M R, Redinbo, S M, Eide, R L, Stone, J E, Dixon, T O, Yeates

Publikováno v: Protein science : a publication of the Protein Society. 5(4)

Adenylosuccinate lyase (ASL) from Bacillus subtilis has been crystallized and structural analysis by X-ray diffraction is in progress. ASL is a 200-kDa homotetramer that catalyzes two distinct steps of de novo purine biosynthesis leading to the forma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::327001f44b753bc158d57d831da5bc61
https://pubmed.ncbi.nlm.nih.gov/8845770

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Crystallization and preliminary structural studies of neurotrophin-3

Autor: J A, Kelly, E, Singer, T D, Osslund, T O, Yeates

Publikováno v: Protein science : a publication of the Protein Society. 3(6)

Neurotrophin-3 (NT-3) has been crystallized in 2 forms. Orthorhombic crystals, space group P2(1)2(1)2, diffracted to 2.8 A and have cell dimensions a = 39.1 A, b = 54.0 A, and c = 65.5 A. The second form is space group P4(3)2(1)2, with cell dimension

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::695cb535501811c3bd4bdb58b80b2bc3
https://pubmed.ncbi.nlm.nih.gov/8069227

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