A three-dimensional model of domain III of the Escherichia coli small ribosomal subunit

ABSTRACT The replacement of M74 in GyrA, A83 in GyrA, and R447 in GyrB of Mycobacterium tuberculosis gyrase by their Escherichia coli homologs resulted in active enzymes as quinolone susceptible as the E. coli gyrase. This demonstrates that the primary structure of gyrase determines intrinsic quinolone resistance and was supported by a three-dimensional model of N-terminal GyrA.

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Three-dimensional Model of Escherichia coli Gyrase B Subunit Crystallized in Two-dimensions on Novobiocin-Linked Phospholipid Films

Journal of Molecular Biology ◽

10.1006/jmbi.1994.1171 ◽

1994 ◽

Vol 236 (2) ◽

pp. 618-628 ◽

Cited By ~ 28

Author(s):

Hervé Celia ◽

Laurence Hoermann ◽

Patrick Schultz ◽

Luc Lebeau ◽

Véronique Mallouh ◽

...

Keyword(s):

Escherichia Coli ◽

Three Dimensional ◽

Two Dimensions ◽

Dimensional Model ◽

Three Dimensional Model ◽

B Subunit

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Three-dimensional model for the membrane domain of Escherichia coli leader peptidase based on disulfide mapping

Biochemistry ◽

10.1021/bi00084a020 ◽

1993 ◽

Vol 32 (33) ◽

pp. 8534-8539 ◽

Cited By ~ 41

Author(s):

Paul Whitley ◽

Lennart Nilsson ◽

Gunnar von Heijne

Keyword(s):

Escherichia Coli ◽

Three Dimensional ◽

Membrane Domain ◽

Dimensional Model ◽

Three Dimensional Model ◽

Leader Peptidase

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Structural organization of escherichia coli ribosomes as determined by immuno electron microscopy

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100081693 ◽

1978 ◽

Vol 36 (2) ◽

pp. 166-167 ◽

Cited By ~ 1

Author(s):

G. Stöffler ◽

R.W. Bald ◽

J. Dieckhoff ◽

H. Eckhard ◽

R. Lührmann ◽

...

Keyword(s):

Electron Microscopy ◽

Escherichia Coli ◽

Ribosomal Proteins ◽

Structural Organization ◽

Three Dimensional ◽

Ribosomal Subunit ◽

Spatial Arrangement ◽

Small Subunit ◽

Antibody Binding ◽

Immuno Electron Microscopy

A central step towards an understanding of the structure and function of the Escherichia coli ribosome, a large multicomponent assembly, is the elucidation of the spatial arrangement of its 54 proteins and its three rRNA molecules. The structural organization of ribosomal components has been investigated by a number of experimental approaches. Specific antibodies directed against each of the 54 ribosomal proteins of Escherichia coli have been performed to examine antibody-subunit complexes by electron microscopy. The position of the bound antibody, specific for a particular protein, can be determined; it indicates the location of the corresponding protein on the ribosomal surface.The three-dimensional distribution of each of the 21 small subunit proteins on the ribosomal surface has been determined by immuno electron microscopy: the 21 proteins have been found exposed with altogether 43 antibody binding sites. Each one of 12 proteins showed antibody binding at remote positions on the subunit surface, indicating highly extended conformations of the proteins concerned within the 30S ribosomal subunit; the remaining proteins are, however, not necessarily globular in shape (Fig. 1).

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