Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site

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Standard

Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. / Laurberg, M; Kristensen, Ole; Martemyanov, K; Gudkov, A T; Nagaev, I; Hughes, D; Liljas, A.

In: Journal of Molecular Biology, Vol. 303, No. 4, 2000, p. 593-603.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Laurberg, M, Kristensen, O, Martemyanov, K, Gudkov, AT, Nagaev, I, Hughes, D & Liljas, A 2000, 'Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site', Journal of Molecular Biology, vol. 303, no. 4, pp. 593-603. https://doi.org/10.1006/jmbi.2000.4168

APA

Laurberg, M., Kristensen, O., Martemyanov, K., Gudkov, A. T., Nagaev, I., Hughes, D., & Liljas, A. (2000). Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. Journal of Molecular Biology, 303(4), 593-603. https://doi.org/10.1006/jmbi.2000.4168

Vancouver

Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D et al. Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. Journal of Molecular Biology. 2000;303(4):593-603. https://doi.org/10.1006/jmbi.2000.4168

Author

Laurberg, M ; Kristensen, Ole ; Martemyanov, K ; Gudkov, A T ; Nagaev, I ; Hughes, D ; Liljas, A. / Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. In: Journal of Molecular Biology. 2000 ; Vol. 303, No. 4. pp. 593-603.

Bibtex

@article{232df994ffe74ad8906bb8c4ed5756b1,
title = "Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site",
abstract = "The crystal structure of Thermus thermophilus elongation factor G (EF-G) carrying the point mutation His573Ala was determined at a resolution of 2.8 A. The mutant has a more closed structure than that previously reported for wild-type EF-G. This is obtained by a 10 degrees rigid rotation of domains III, IV and V with regard to domains I and II. This rotation results in a displacement of the tip of domain IV by approximately 9 A. The structure of domain III is now fully visible and reveals the double split beta-alpha-beta motif also observed for EF-G domain V and for several ribosomal proteins. A large number of fusidic acid resistant mutations found in domain III have now been possible to locate. Possible locations for the effector loop and a possible binding site for fusidic acid are discussed in relation to some of the fusidic acid resistant mutations.",
keywords = "Amino Acid Motifs, Amino Acid Sequence, Amino Acid Substitution, Binding Sites, Conserved Sequence, Crystallography, X-Ray, Drug Resistance, Microbial, Fusidic Acid, Guanosine Diphosphate, Models, Molecular, Molecular Sequence Data, Peptide Elongation Factor G, Point Mutation, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Alignment, Thermus thermophilus",
author = "M Laurberg and Ole Kristensen and K Martemyanov and Gudkov, {A T} and I Nagaev and D Hughes and A Liljas",
note = "Copyright 2000 Academic Press.",
year = "2000",
doi = "10.1006/jmbi.2000.4168",
language = "English",
volume = "303",
pages = "593--603",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press",
number = "4",

}

RIS

TY - JOUR

T1 - Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site

AU - Laurberg, M

AU - Kristensen, Ole

AU - Martemyanov, K

AU - Gudkov, A T

AU - Nagaev, I

AU - Hughes, D

AU - Liljas, A

N1 - Copyright 2000 Academic Press.

PY - 2000

Y1 - 2000

N2 - The crystal structure of Thermus thermophilus elongation factor G (EF-G) carrying the point mutation His573Ala was determined at a resolution of 2.8 A. The mutant has a more closed structure than that previously reported for wild-type EF-G. This is obtained by a 10 degrees rigid rotation of domains III, IV and V with regard to domains I and II. This rotation results in a displacement of the tip of domain IV by approximately 9 A. The structure of domain III is now fully visible and reveals the double split beta-alpha-beta motif also observed for EF-G domain V and for several ribosomal proteins. A large number of fusidic acid resistant mutations found in domain III have now been possible to locate. Possible locations for the effector loop and a possible binding site for fusidic acid are discussed in relation to some of the fusidic acid resistant mutations.

AB - The crystal structure of Thermus thermophilus elongation factor G (EF-G) carrying the point mutation His573Ala was determined at a resolution of 2.8 A. The mutant has a more closed structure than that previously reported for wild-type EF-G. This is obtained by a 10 degrees rigid rotation of domains III, IV and V with regard to domains I and II. This rotation results in a displacement of the tip of domain IV by approximately 9 A. The structure of domain III is now fully visible and reveals the double split beta-alpha-beta motif also observed for EF-G domain V and for several ribosomal proteins. A large number of fusidic acid resistant mutations found in domain III have now been possible to locate. Possible locations for the effector loop and a possible binding site for fusidic acid are discussed in relation to some of the fusidic acid resistant mutations.

KW - Amino Acid Motifs

KW - Amino Acid Sequence

KW - Amino Acid Substitution

KW - Binding Sites

KW - Conserved Sequence

KW - Crystallography, X-Ray

KW - Drug Resistance, Microbial

KW - Fusidic Acid

KW - Guanosine Diphosphate

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Peptide Elongation Factor G

KW - Point Mutation

KW - Protein Structure, Secondary

KW - Protein Structure, Tertiary

KW - Sequence Alignment

KW - Thermus thermophilus

U2 - 10.1006/jmbi.2000.4168

DO - 10.1006/jmbi.2000.4168

M3 - Journal article

C2 - 11054294

VL - 303

SP - 593

EP - 603

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 4

ER -

ID: 47416685