Crystal structure of the Glu-239 → Gln mutant of aspartate carbamoyltransferase at 3.1-Å resolution: An intermediate quaternary structure

Eric Gouaux, R. C. Stevens, H. Ke, W. N. Lipscomb

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Abstract

The structure of the unligated Glu 239 → Gln mutant of Escherichia coli aspartate carbamoyltransferase (EC 2.1.3.2) has been determined to 3.1-Å resolution and refined to a crystallographic residual of 0.22 in the space group P321. The unit-cell dimensions of the unligated enzyme are a = 122.3 Å, c = 147.1 Å. The c axis cell length is intermediate between the c axis lengths of the T (tense) (c = 142.2 Å) and R (relaxed) (c = 156.2 Å) state structures. Furthermore, the quaternary structure of the mutant enzyme is intermediate between the quaternary structures of the T form and the R form. The differences between the quaternary structures of the Glu-239 → Gln and T-form enzymes can be described as follows: the separation between the catalytic trimers increases by ≃ 1.5 Å along the threefold axis, and they each rotate in opposite directions ≃ 0.5° around the threefold axis, whereas the regulatory dimers rotate ≃ 2° around the twofold axes.

Original languageEnglish (US)
Pages (from-to)8212-8216
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume86
Issue number21
StatePublished - 1989
Externally publishedYes

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Aspartate Carbamoyltransferase
Enzymes
Escherichia coli

ASJC Scopus subject areas

  • General
  • Genetics

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title = "Crystal structure of the Glu-239 → Gln mutant of aspartate carbamoyltransferase at 3.1-{\AA} resolution: An intermediate quaternary structure",
abstract = "The structure of the unligated Glu 239 → Gln mutant of Escherichia coli aspartate carbamoyltransferase (EC 2.1.3.2) has been determined to 3.1-{\AA} resolution and refined to a crystallographic residual of 0.22 in the space group P321. The unit-cell dimensions of the unligated enzyme are a = 122.3 {\AA}, c = 147.1 {\AA}. The c axis cell length is intermediate between the c axis lengths of the T (tense) (c = 142.2 {\AA}) and R (relaxed) (c = 156.2 {\AA}) state structures. Furthermore, the quaternary structure of the mutant enzyme is intermediate between the quaternary structures of the T form and the R form. The differences between the quaternary structures of the Glu-239 → Gln and T-form enzymes can be described as follows: the separation between the catalytic trimers increases by ≃ 1.5 {\AA} along the threefold axis, and they each rotate in opposite directions ≃ 0.5° around the threefold axis, whereas the regulatory dimers rotate ≃ 2° around the twofold axes.",
author = "Eric Gouaux and Stevens, {R. C.} and H. Ke and Lipscomb, {W. N.}",
year = "1989",
language = "English (US)",
volume = "86",
pages = "8212--8216",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
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TY - JOUR

T1 - Crystal structure of the Glu-239 → Gln mutant of aspartate carbamoyltransferase at 3.1-Å resolution

T2 - An intermediate quaternary structure

AU - Gouaux, Eric

AU - Stevens, R. C.

AU - Ke, H.

AU - Lipscomb, W. N.

PY - 1989

Y1 - 1989

N2 - The structure of the unligated Glu 239 → Gln mutant of Escherichia coli aspartate carbamoyltransferase (EC 2.1.3.2) has been determined to 3.1-Å resolution and refined to a crystallographic residual of 0.22 in the space group P321. The unit-cell dimensions of the unligated enzyme are a = 122.3 Å, c = 147.1 Å. The c axis cell length is intermediate between the c axis lengths of the T (tense) (c = 142.2 Å) and R (relaxed) (c = 156.2 Å) state structures. Furthermore, the quaternary structure of the mutant enzyme is intermediate between the quaternary structures of the T form and the R form. The differences between the quaternary structures of the Glu-239 → Gln and T-form enzymes can be described as follows: the separation between the catalytic trimers increases by ≃ 1.5 Å along the threefold axis, and they each rotate in opposite directions ≃ 0.5° around the threefold axis, whereas the regulatory dimers rotate ≃ 2° around the twofold axes.

AB - The structure of the unligated Glu 239 → Gln mutant of Escherichia coli aspartate carbamoyltransferase (EC 2.1.3.2) has been determined to 3.1-Å resolution and refined to a crystallographic residual of 0.22 in the space group P321. The unit-cell dimensions of the unligated enzyme are a = 122.3 Å, c = 147.1 Å. The c axis cell length is intermediate between the c axis lengths of the T (tense) (c = 142.2 Å) and R (relaxed) (c = 156.2 Å) state structures. Furthermore, the quaternary structure of the mutant enzyme is intermediate between the quaternary structures of the T form and the R form. The differences between the quaternary structures of the Glu-239 → Gln and T-form enzymes can be described as follows: the separation between the catalytic trimers increases by ≃ 1.5 Å along the threefold axis, and they each rotate in opposite directions ≃ 0.5° around the threefold axis, whereas the regulatory dimers rotate ≃ 2° around the twofold axes.

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JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

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