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PDBsum entry 3e2p
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References listed in PDB file
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Key reference
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Title
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Structure of the catalytic trimer of methanococcus jannaschii aspartate transcarbamoylase in an orthorhombic crystal form.
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Authors
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J.Vitali,
M.J.Colaneri.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008,
64,
776-780.
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PubMed id
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Abstract
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Crystals of the catalytic subunit of Methanococcus jannaschii aspartate
transcarbamoylase in an orthorhombic crystal form contain four
crystallographically independent trimers which associate in pairs to form stable
staggered complexes that are similar to each other and to a previously
determined monoclinic C2 form. Each subunit has a sulfate in the central
channel. The catalytic subunits in these complexes show flexibility, with the
elbow angles of the monomers differing by up to 7.4 degrees between crystal
forms. Moreover, there is also flexibility in the relative orientation of the
trimers around their threefold axis in the complexes, with a difference of 4
degrees between crystal forms.
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Secondary reference #1
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Title
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Crystal structure of the catalytic trimer of methanococcus jannaschii aspartate transcarbamoylase.
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Authors
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J.Vitali,
M.J.Colaneri,
E.Kantrowitz.
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Ref.
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Proteins, 2007,
71,
1324-1334.
[DOI no: ]
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PubMed id
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Figure 4.
Figure 4. (a) Complexation of a sulfate ion on the three-fold
axis by three Lys residues (Lys63) from the three chains of the
trimer. View is along the threefold axis. Three of the sulfate
oxygens are related by the threefold axis. The fourth, not
shown, lies on the threefold axis. (b) View of the ion-pair
network in the central channel centered on the sulfate ion. The
electron density corresponds to the final sigmaa weighted 2Fo -
Fc map, is drawn at a contour level of 1.0  and
is carved around the sulfate, Lys63, Glu59, and Arg55.
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Figure 6.
Figure 6. Ion pair networks at the C1-C2 type interfaces.
Colors of the chains are as in Figure 3.
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The above figures are
reproduced from the cited reference
with permission from John Wiley & Sons, Inc.
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