New crystal forms of glutamine synthetase and implications for the molecular structure

E. G. Heidner, T. G. Frey, J. Held, L. J. Weissman, R. E. Fenna, M. Lei, M. Harel, H. Kabsch, R. M. Sweet, D. Eisenberg

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

New crystal forms of glutamine synthetase from Escherichia coli are reported. Two of these (II A and II B) demand that the dodecameric molecule contains a 2-fold axis of symmetry perpendicular to the apparent hexagonal face. Whereas forms II A and II B and others reported previously (I and III A) were grown from enzyme containing covalently bound AMP groups, a third new form (III C) was grown from enzyme lacking covalently bound AMP groups. Form III C is isomorphous with form III A. This demonstrates that the addition of AMP groups, which profoundly affect the catalytic and regulatory properties of glutamine synthetase, does not alter the dimensions of the molecular envelope. Thus adenylylation of the enzyme does not seem to cause a quaternary structural transition, though small changes of intensities suggest that there may be tertiary structural changes within the subunits. Other new forms include form III B, a low symmetry polymorph, closely related to form III A, and form IV, a trigonal polymorph with large asymmetric unit. All crystal forms are consistent with a symmetry of 622 for the glutamine synthetase molecule.

Original languageEnglish (US)
Pages (from-to)163-173
Number of pages11
JournalJournal of Molecular Biology
Volume122
Issue number2
DOIs
StatePublished - Jun 25 1978

Fingerprint

Glutamate-Ammonia Ligase
Adenosine Monophosphate
Molecular Structure
Enzymes
Escherichia coli

ASJC Scopus subject areas

  • Virology

Cite this

New crystal forms of glutamine synthetase and implications for the molecular structure. / Heidner, E. G.; Frey, T. G.; Held, J.; Weissman, L. J.; Fenna, R. E.; Lei, M.; Harel, M.; Kabsch, H.; Sweet, R. M.; Eisenberg, D.

In: Journal of Molecular Biology, Vol. 122, No. 2, 25.06.1978, p. 163-173.

Research output: Contribution to journalArticle

Heidner, EG, Frey, TG, Held, J, Weissman, LJ, Fenna, RE, Lei, M, Harel, M, Kabsch, H, Sweet, RM & Eisenberg, D 1978, 'New crystal forms of glutamine synthetase and implications for the molecular structure', Journal of Molecular Biology, vol. 122, no. 2, pp. 163-173. https://doi.org/10.1016/0022-2836(78)90033-5
Heidner, E. G. ; Frey, T. G. ; Held, J. ; Weissman, L. J. ; Fenna, R. E. ; Lei, M. ; Harel, M. ; Kabsch, H. ; Sweet, R. M. ; Eisenberg, D. / New crystal forms of glutamine synthetase and implications for the molecular structure. In: Journal of Molecular Biology. 1978 ; Vol. 122, No. 2. pp. 163-173.
@article{965d703a55dd4c30bc9bf33c785eced4,
title = "New crystal forms of glutamine synthetase and implications for the molecular structure",
abstract = "New crystal forms of glutamine synthetase from Escherichia coli are reported. Two of these (II A and II B) demand that the dodecameric molecule contains a 2-fold axis of symmetry perpendicular to the apparent hexagonal face. Whereas forms II A and II B and others reported previously (I and III A) were grown from enzyme containing covalently bound AMP groups, a third new form (III C) was grown from enzyme lacking covalently bound AMP groups. Form III C is isomorphous with form III A. This demonstrates that the addition of AMP groups, which profoundly affect the catalytic and regulatory properties of glutamine synthetase, does not alter the dimensions of the molecular envelope. Thus adenylylation of the enzyme does not seem to cause a quaternary structural transition, though small changes of intensities suggest that there may be tertiary structural changes within the subunits. Other new forms include form III B, a low symmetry polymorph, closely related to form III A, and form IV, a trigonal polymorph with large asymmetric unit. All crystal forms are consistent with a symmetry of 622 for the glutamine synthetase molecule.",
author = "Heidner, {E. G.} and Frey, {T. G.} and J. Held and Weissman, {L. J.} and Fenna, {R. E.} and M. Lei and M. Harel and H. Kabsch and Sweet, {R. M.} and D. Eisenberg",
year = "1978",
month = "6",
day = "25",
doi = "10.1016/0022-2836(78)90033-5",
language = "English (US)",
volume = "122",
pages = "163--173",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - New crystal forms of glutamine synthetase and implications for the molecular structure

AU - Heidner, E. G.

AU - Frey, T. G.

AU - Held, J.

AU - Weissman, L. J.

AU - Fenna, R. E.

AU - Lei, M.

AU - Harel, M.

AU - Kabsch, H.

AU - Sweet, R. M.

AU - Eisenberg, D.

PY - 1978/6/25

Y1 - 1978/6/25

N2 - New crystal forms of glutamine synthetase from Escherichia coli are reported. Two of these (II A and II B) demand that the dodecameric molecule contains a 2-fold axis of symmetry perpendicular to the apparent hexagonal face. Whereas forms II A and II B and others reported previously (I and III A) were grown from enzyme containing covalently bound AMP groups, a third new form (III C) was grown from enzyme lacking covalently bound AMP groups. Form III C is isomorphous with form III A. This demonstrates that the addition of AMP groups, which profoundly affect the catalytic and regulatory properties of glutamine synthetase, does not alter the dimensions of the molecular envelope. Thus adenylylation of the enzyme does not seem to cause a quaternary structural transition, though small changes of intensities suggest that there may be tertiary structural changes within the subunits. Other new forms include form III B, a low symmetry polymorph, closely related to form III A, and form IV, a trigonal polymorph with large asymmetric unit. All crystal forms are consistent with a symmetry of 622 for the glutamine synthetase molecule.

AB - New crystal forms of glutamine synthetase from Escherichia coli are reported. Two of these (II A and II B) demand that the dodecameric molecule contains a 2-fold axis of symmetry perpendicular to the apparent hexagonal face. Whereas forms II A and II B and others reported previously (I and III A) were grown from enzyme containing covalently bound AMP groups, a third new form (III C) was grown from enzyme lacking covalently bound AMP groups. Form III C is isomorphous with form III A. This demonstrates that the addition of AMP groups, which profoundly affect the catalytic and regulatory properties of glutamine synthetase, does not alter the dimensions of the molecular envelope. Thus adenylylation of the enzyme does not seem to cause a quaternary structural transition, though small changes of intensities suggest that there may be tertiary structural changes within the subunits. Other new forms include form III B, a low symmetry polymorph, closely related to form III A, and form IV, a trigonal polymorph with large asymmetric unit. All crystal forms are consistent with a symmetry of 622 for the glutamine synthetase molecule.

UR - http://www.scopus.com/inward/record.url?scp=0017803554&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017803554&partnerID=8YFLogxK

U2 - 10.1016/0022-2836(78)90033-5

DO - 10.1016/0022-2836(78)90033-5

M3 - Article

C2 - 28418

AN - SCOPUS:0017803554

VL - 122

SP - 163

EP - 173

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 2

ER -