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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

Active-centre torsion-angle strain revealed in 1.6 angstrom-resolution structure of histidine-containing phosphocarrier protein

Article Abstract:

Carbohydrate transport across bacterial cell membranes involves the histidine-containing phosphocarrier protein (HPr). X-ray crystallography allowed determining the structure of HPr at 1.6 angstrom resolution. Ramachandran torsion angles were found at the active center of the molecule which are probably involved in the transport function. Independent research yields direct evidence in support of this contention and suggests that there is an HPr cycling mechanism driven by phototransferase and HPr structures.

Author: Jia, Zongchao, Vandonselaar, Margaret, Quail, J. Wilson, Delbaere, Louis T.J.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
Usage, Biological transport, Active, Active biological transport, Cell membranes, X-ray crystallography, Phosphotransferases

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Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule-1 at 1.8 angstrom resolution

Article Abstract:

A fragment constituting the first two domains of the cell-surface glycoprotein vascular cell adhesion molecule-1 that binds to the very-late antigen-4 (VLA-4) contains an exposed integrin-binding motif. This motif is present in all such integrin-molecules and acts as the N-terminal region of the loop between the beta-strands C and D of the first domain. The CFG beta-sheet faces the VLA-4 binding site.

Author: Robinson, R.C., Jones, E.Y., Harlos, K., Bottomley M.J., Driscoll, P.C., Edwards, R.M., Clements, J.M., Dudgeon, T.J., Stuart, D.I.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
Cell adhesion molecules, Crystals, Crystal structure

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Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 angstrom resolution

Article Abstract:

X-ray investigations of the crystal structure of the molecular complex of penicillin G with beta-lactamase from Escherichia coli reveals how such beta-lactam antibodies are recognized and destroyed. The penicillin G binds to Ser 70 O(super gamma) as an intermediate. These structures are illustrated.

Author: Strynadka, Natalie C.J., Jensen, Susan E., Adachi, Hiroyuki, Johns, Kathy, Sielecki, Anita, Betzel, Christian, Sutoh, Kazuo, James, Michael N.G.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
Antibiotic structure-activity relationships, Beta lactam antibiotics

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Subjects list: Research
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