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PDBsum entry 5d6j
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Ligase/protein binding
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PDB id
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5d6j
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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 fadd32, An enzyme essential for mycolic acid biosynthesis in mycobacteria.
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Authors
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W.Li,
S.Gu,
J.Fleming,
L.Bi.
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Ref.
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Sci Rep, 2015,
5,
15493.
[DOI no: ]
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PubMed id
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Abstract
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Fatty acid degradation protein D32 (FadD32), an enzyme required for mycolic acid
biosynthesis and essential for mycobacterial growth, has recently been
identified as a valid and promising target for anti-tuberculosis drug
development. Here we report the crystal structures of Mycobacterium smegmatis
FadD32 in the apo and ATP-bound states at 2.4 Å and 2.25 Å resolution,
respectively. FadD32 consists of two globular domains connected by a flexible
linker. ATP binds in a cleft at the interface between the N- and C-terminal
domains and its binding induces significant local conformational changes in
FadD32. The binding sites of meromycolic acid and phosphopantetheine are
identified by structural comparison with other members of the adenylating enzyme
superfamily. These results will improve our understanding of the catalytic
mechanism of FadD32 and help in the design of inhibitors of this essential
enzyme.
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