Zobrazeno 1 - 10 of 13 pro vyhledávání: '"Mohammed O, Badasso"'
1
Bacteriophage φ29 scaffolding protein gp7 before and after prohead assembly
Autor: Dwight L. Anderson, Shuji Kanamaru, Mohammed O. Badasso, Jaya S. Koti, Barbara A.L. Owen, Marc C. Morais, Cynthia T. McMurray, Michael G. Rossmann
Publikováno v: Nature Structural & Molecular Biology. 10:572-576
Three-dimensional structures of the double-stranded DNA bacteriophage phi29 scaffolding protein (gp7) before and after prohead assembly have been determined at resolutions of 2.2 and 2.8 A, respectively. Both structures are dimers that resemble arrow
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f77043ea5675bab862283a44e853cb16
https://doi.org/10.1038/nsb939
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4
Structure of the bacteriophage φ29 DNA packaging motor
Autor: Norman H. Olson, Petr G. Leiman, Mohammed O. Badasso, Paul J. Jardine, Timothy S. Baker, Yizhi Jane Tao, Marc C. Morais, Dwight L. Anderson, Alan A. Simpson, Michael G. Rossmann, Yongning He, Shelley Grimes
Publikováno v: Nature. 408:745-750
Motors generating mechanical force, powered by the hydrolysis of ATP, translocate double-stranded DNA into preformed capsids (proheads) of bacterial viruses and certain animal viruses. Here we describe the motor that packages the double-stranded DNA
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e787ea3016621189eb0b9391138a7472
https://doi.org/10.1038/35047129
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5
X-ray structures of five renin inhibitors bound to saccharopepsin: exploration of active-site specificity 1 1Edited by R. Huber
Autor: Elizabeth A. Lunney, Robert L. Rosati, Dennis J. Hoover, Ian J. Tickle, Mohammed O. Badasso, Christine Humblet, T. Dreyer, Jonathan B. Cooper, Nora Cronin
Publikováno v: Journal of Molecular Biology. 303:745-760
Saccharopepsin is a vacuolar aspartic proteinase involved in activation of a number of hydrolases. The enzyme has great structural homology to mammalian aspartic proteinases including human renin and we have used it as a model system to study the bin
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fdd8afd6ff52349b4335d63c22274122
https://doi.org/10.1006/jmbi.2000.4181
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6
A 2.3 A resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site beta-hairpin flap is rearranged when compared with the native crystal structure
Autor: Dennis J. Hoover, Mohammed O. Badasso, Philip Nugent, Tom L. Blundell, V. Dhanaraj, J. E. Pitts, Matthew Groves
Publikováno v: University of Groningen
Protein Engineering, 11(10), 833-840
In the crystal structure of uncomplexed native chymosin, the beta-hairpin at the active site, known as 'the flap', adopts a different conformation from that of other aspartic proteinases. This conformation would prevent the mode of binding of substra
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fee8fd6d169af041c07b6f849fe8896
https://doi.org/10.1093/protein/11.10.833
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7
Crystallization and initial X-ray diffraction studies of scaffolding protein (gp7) of bacteriophage ϕ29
Autor: Dwight L. Anderson, Mohammed O. Badasso
Publikováno v: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61:424-426
The Bacillus subtilis bacteriophage phi29 scaffolding protein (gp7) has been crystallized by the hanging-drop vapour-diffusion method at 293 K. Two new distinct crystal forms that both differed from a previously crystallized and solved scaffolding pr
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4380db16c1fe9973006a5eec861cbf5
https://doi.org/10.1107/s1744309105008511
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8
Crystallization and X-ray analysis of the Y75N mutant of Mucor pusillus pepsin complexed with inhibitor
Autor: Jonathan B. Cooper, Tom L. Blundell, V. Dhanaraj, Mohammed O. Badasso, Steve P. Wood
Publikováno v: Acta crystallographica. Section D, Biological crystallography. 60(Pt 4)
Y75N mutant Mucor pusillus pepsin has been overexpressed in yeast, purified and cocrystallized with the iodine-containing human renin inhibitor CP-113972 [(2R,3S]-isopropyl 3-[(L-prolyl-p-iodo-L-phenylalanyl-S-methyl-cysteinyl)amino-4]-cyclohexyl-2-h
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53a0e13ea3833dd3f9e20271c314032b
https://pubmed.ncbi.nlm.nih.gov/15039581
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9
Purification, crystallization and initial X-ray analysis of the head-tail connector of bacteriophage phi29
Autor: Petr G. Leiman, Mohammed O. Badasso, Douglas H. Ohlendorf, Yizhi Tao, Yongning He, Dwight L. Anderson, Michael G. Rossmann
Publikováno v: Acta crystallographica. Section D, Biological crystallography. 56(Pt 9)
The head-tail connector of bacteriophage phi29, an oligomer of gene product 10 (gp10), was crystallized into various forms. The most useful of these were an orthorhombic P22(1)2(1) form (unit-cell parameters a = 143.0, b = 157.0, c = 245.2 A), a mono
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8fd026bc41412b8e1a452074fc578cb
https://pubmed.ncbi.nlm.nih.gov/10957642
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10
Purification, co-crystallization and preliminary X--ray analysis of the natural aspartic proteinase inhibitor IA3 complexed with saccharopepsin from Saccharomyces cerevisiae
Autor: Jonathan B. Cooper, Jakob R. Winther, Steve P. Wood, Mohammed O. Badasso, J.A. Read, Tom L. Blundell, T. Dreyer, V. Dhanaraj
Publikováno v: Acta crystallographica. Section D, Biological crystallography. 56(Pt 7)
The vacuolar aspartic proteinase from baker's yeast, saccharopepsin, has been co-crystallized with its natural inhibitor I(A)3, found in the cytosol. The I(A)3-saccharopepsin complex crystals belong to the space group P6(2)22, with unit-cell paramete
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::010583c8f5a10abef796f4a9fd54811a
https://pubmed.ncbi.nlm.nih.gov/10930843
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