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PDBsum entry 1qnq
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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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The three-Dimensional structure of a trichoderma reesei beta-Mannanase from glycoside hydrolase family 5.
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Authors
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E.Sabini,
H.Schubert,
G.Murshudov,
K.S.Wilson,
M.Siika-Aho,
M.Penttilä.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2000,
56,
3.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of the catalytic core domain of beta-mannanase from the
fungus Trichoderma reesei has been determined at a resolution of 1.5 A. The
structure was solved using the anomalous scattering from a single
non-isomorphous platinum complex with two heavy-metal sites in space group
P2(1). The map computed with the experimental phases was enhanced by the
application of an automated model building and refinement procedure using the
amplitudes and experimental phases as observations. This approach is expected to
be of more general application. The structure of the native enzyme and complexes
with Tris-HCl and mannobiose are also reported: the mannobiose binds in subsites
+1 and +2. The structure is briefly compared with that of the homologous
beta-mannanase from the bacterium Thermomonospora fusca.
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Figure 1.
Figure 1 (a) Anomalous and (b) isomorphous difference Patterson
syntheses at 1.65 Å resolution for the Pty complex: the Harker
vectors of the two platinum sites are indicated.
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Figure 5.
Figure 5 As Fig. 4-. Aromatic residues (here Trp164 is shown)
had a `hole' at the centre of the ring in the REFMAC/ARP map (c).
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2000,
56,
3-0)
copyright 2000.
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