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PDBsum entry 2c1h
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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 chlorobium vibrioforme 5-Aminolaevulinic acid dehydratase complexed with a diacid inhibitor.
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Authors
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L.Coates,
G.Beaven,
P.T.Erskine,
S.I.Beale,
S.P.Wood,
P.M.Shoolingin-Jordan,
J.B.Cooper.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2005,
61,
1594-1598.
[DOI no: ]
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PubMed id
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Abstract
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The structure of Chlorobium vibrioforme 5-aminolaevulinic acid dehydratase
(ALAD) complexed with the irreversible inhibitor 4,7-dioxosebacic acid has been
solved. The inhibitor binds by forming Schiff-base linkages with lysines 200 and
253 at the active site. The structure reported here provides a definition of the
interactions made by both of the substrate molecules (A-side and P-side
substrates) with the C. vibrioforme ALAD and is compared and contrasted with
structures of the same inhibitor bound to Escherichia coli and yeast ALAD. The
structure suggests why 4,7-dioxosebacic acid is a better inhibitor of the
zinc-dependent ALADs than of the zinc-independent ALADs.
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Figure 1.
Figure 1
The reaction catalysed by 5-aminolaevulinic acid dehydratase (ALAD). Two molecules of
5-aminolaevulinic acid are condensed to form the pyrrole porphobilinogen.
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Figure 3.
Figure 3
(a) The 2F[o] - F[c] [168][sigma] [A]-weighted electron-density map (shown in cyan) for
the inhibitor 4,7-dioxosebacic acid at 2.60 Å resolution. The covalent bonds between the
inhibitor and lysines 200 and 253 are also shown. (b) The hydrogen bonds made by the
carboxyl groups of the inhibitor with surrounding residues (donor-acceptor distances are
shown in Å). The atoms labelled C4 and C7 are attached to the invariant lysine residues by
Schiff bases. In both (a) and (b) the map is contoured at 1.25 r.m.s. and the A-site of
the enzyme is on the left-hand side, with the P-site on the right.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2005,
61,
1594-1598)
copyright 2005.
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