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PDBsum entry 4u72
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Oxidoreductase
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PDB id
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4u72
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References listed in PDB file
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Key reference
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Title
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Conformation and mobility of active site loop is crit for substrate binding and inhibition in human indolea 2,3-Dioxygenase
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Authors
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M.Horitani,
E.Kometani,
E.Vottero,
T.Otsuki,
Y.Shiro,
H.Su.
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Ref.
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TO BE PUBLISHED ...
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Secondary reference #1
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Title
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Crystal structure of human indoleamine 2,3-Dioxygenase: catalytic mechanism of o2 incorporation by a heme-Containing dioxygenase.
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Authors
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H.Sugimoto,
S.Oda,
T.Otsuki,
T.Hino,
T.Yoshida,
Y.Shiro.
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Ref.
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Proc Natl Acad Sci U S A, 2006,
103,
2611-2616.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. Structure of IDO–PI complex. (A) Ribbon
representation of the overall structure of human IDO. The small
and large domains are represented by blue and green ribbons,
respectively. The helices A–S are named in the order of
appearance in the primary sequence. The connecting helices (K-L
and N) are colored in cyan. The long loop connecting the two
domains is colored in red. The heme (yellow), proximal ligand
H346 (white), and heme inhibitor 4-phynylimidazole (white) are
shown in a ball-and-stick model. The helices of the large domain
create the cavity for the heme. The connecting loop (red) and
small domain above the sixth-coordination site (heme distal
side) cover the top of cavity on the heme. (B) The four proximal
helices I, G, Q, and S run in parallel. The helices N (blue) and
K-L (cyan) connect the two domains. The connecting loop (red)
and small domain above the sixth-coordination site of the heme
cover the top of the cavity on the heme.
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Figure 3.
Fig. 3. Active site of IDO–PI complex. (A) Stereoview of
the residues around the heme of IDO viewed from the side of heme
plane. The proximal ligand H346 is H-bonded to wa1. The
6-propionate of the heme contacts with wa2 and R343 N  . The
wa2 is H-bonded to wa1, L388 O, and 6-propionate. Mutations of
F226, F227, and R231 do not lose the substrate affinity but
produce the inactive enzyme. Two CHES molecules are bound in the
distal pocket. The cyclohexan ring of CHES-1 (green) contacts
with F226 and R231. The 7-propionate of the heme interacts with
the amino group of CHES-1 and side chain of Ser-263. The
mutational analyses for these distal residues are shown in Table
1. (B) Top view of A by a rotation of 90°. The proximal
residues are omitted.
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