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PDBsum entry 1vk3
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of phosphoribosylformylglycinamidine synthase ii (smpurl) from thermotoga maritima at 2.15 a resolution.
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Authors
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I.I.Mathews,
S.S.Krishna,
R.Schwarzenbacher,
D.Mcmullan,
P.Abdubek,
E.Ambing,
J.M.Canaves,
H.J.Chiu,
A.M.Deacon,
M.Didonato,
M.A.Elsliger,
A.Godzik,
C.Grittini,
S.K.Grzechnik,
J.Hale,
E.Hampton,
G.W.Han,
J.Haugen,
L.Jaroszewski,
H.E.Klock,
E.Koesema,
A.Kreusch,
P.Kuhn,
S.A.Lesley,
I.Levin,
M.D.Miller,
K.Moy,
E.Nigoghossian,
J.Paulsen,
K.Quijano,
R.Reyes,
G.Spraggon,
R.C.Stevens,
H.Van den bedem,
J.Velasquez,
A.White,
G.Wolf,
Q.Xu,
K.O.Hodgson,
J.Wooley,
I.A.Wilson.
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Ref.
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Proteins, 2006,
63,
1106-1111.
[DOI no: ]
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PubMed id
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Abstract
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No abstract given.
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Figure 2.
Figure 2. Domain arrangement and structural alignment of smPurL
and lgPurL. A: Domain arrangement of PurM, ThiL, smPurL, and
lgPurL proteins. PurM and ThiL are homodimers. smPurL (gray) and
the central domain of lgPurL (blue) have the same domain
arrangement as a PurM dimer. lgPurL has two additional domains
as compared with smPurL. The N-terminal domain homologous to the
PurS protein is colored green and the C-terminal glutaminase
domain is colored red. B: Stereo ribbon diagram of a
superposition of smPurL (gray) and residues 183-960 of lgPurL
from S. typhimurium (blue). The lgPurL N-terminal domain of
unknown function and the C-terminal glutaminase domain are
colored green and red, respectively. These extra domains of
lgPurL correspond to the PurS (TM1244) and PurQ (TM1245)
proteins in T. maritima. The structures were aligned using the
DALI server.
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Figure 3.
Figure 3. A: Stereo diagram of a close-up of the putative
active site of TM1246 superimposed on the lgPurL structure shown
in ribbon representation. The sulfate ions are from the lgPurL
structure. The start and end regions of the glycine-rich loop in
both the structures are labeled in red. B: Stereo diagram of a
close-up of the lgPurL ADP-binding site superimposed on the
smPurL structure shown in ribbon representation. The ADP moiety
and Mg^2+ ions are from the lgPurL structure. In A and B,
residues are numbered according to TM1246 structure (PDB 1vk3)
and the equivalent residues of lgPurL (PDB 1t3t) are shown in
parentheses.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2006,
63,
1106-1111)
copyright 2006.
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