Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Gour P. Pal"'
Publikováno v:
Proceedings of the National Academy of Sciences. 103:305-310
Bacterial cell-surface attachment of macromolecular complexes maintains the microorganism in close proximity to extracellular substrates and allows for optimal uptake of hydrolytic byproducts. The cellulosome is a large multienzyme complex used by ma
Publikováno v:
Structure. 11:1521-1526
The two Ca2+-dependent cysteine proteases, micro- and m-calpain, are involved in various Ca2+-linked signal pathways but differ markedly in their Ca2+ requirements for activation. We have determined the structure of a micro-like calpain, which has 85
Heme oxygenases (HOs) catalyze the oxidation of heme to biliverdin, carbon monoxide (CO), and free iron. Iron acquisition is critical for invading microorganisms to enable survival and growth. Here we report the crystal structure of ChuS, which displ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5abf5f0bc21f572af9990f8a89ea6f59
https://nrc-publications.canada.ca/eng/view/object/?id=b8b206ca-3a76-4686-b5bf-691de538cd37
https://nrc-publications.canada.ca/eng/view/object/?id=b8b206ca-3a76-4686-b5bf-691de538cd37
Autor:
Katherine C. Yam, Zongchao Jia, Jarrett J. Adams, Holly L. Spencer, Steven P. Smith, Gour P. Pal
Publikováno v:
Acta crystallographica. Section F, Structural biology and crystallization communications. 61(Pt 1)
The high-affinity calcium-mediated type II cohesin-dockerin interaction is responsible for the attachment of the multi-enzyme cellulose-degrading complex, termed the cellulosome, to the cell surface of the thermophilic anaerobe Clostridium thermocell
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 59(Pt 2)
The X-ray structure of m-calpain in the absence of Ca(2+) has been described, but it has not been possible to obtain sufficient mu-calpain for structure determination. Comparison of the two structures is of interest in attempting to understand their
Publikováno v:
The Journal of biological chemistry. 276(50)
Calpain is a heterodimeric Ca(2+)-dependent cysteine protease consisting of a large (80 kDa) catalytic subunit and a small (28 kDa) regulatory subunit. The effects of Ca(2+) on the enzyme include activation, aggregation, and autolysis. They may also
Publikováno v:
FEBS Letters. 279:240-242
Wheat germ contains an inhibitor for proicinase K, called PK13 (M1 ∼ 19600) which simultaneously inhibits α-amylase. PK13 was crystallized, space group P21, α = 43.02 (5) Å, n = 65.18 (7) Å, c = 32.33 (4) Å, β = 112.79 (9), X-ray data were co
Publikováno v:
Proteins. 19(2)
Crystals of a complex of proteinase K (molecular mass, 28,790 Da) with its naturally occurring protein inhibitor PK13 (19,641 Da), have been prepared by a microdialysis technique and modified by hanging drop vapor diffusion against 25% ammonium sulfa
Publikováno v:
FEBS letters. 341(2-3)
Proteinase K forms a 1:1 stable complex with its naturally occurring protein inhibitor, PKI3. The crystal structure of this complex has been determined by a combination of molecular replacement and single isomorphous replacement methods. The model co
Autor:
Gour P. Pal, Alexander Tulinsky, Frederick G. Walz, K. G. Ravichandran, Peter Metcalf, Raghuvir K. Arni
Publikováno v:
Biochemistry. 31(12)
The structure of the Gln25 variant of ribonuclease T1 (RNase T1) crystallized at pH 7 and at high ionic strength has been solved by molecular replacement using the coordinates of the Lys25-RNase T1/2'-guanylic acid (2'GMP) complex at pH 5 [Arni et al