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PDBsum entry 2ayh
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Hydrolase (glucanase)
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PDB id
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2ayh
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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 and molecular structure at 0.16-Nm resolution of the hybrid bacillus endo-1,3-1,4-Beta-D-Glucan 4-Glucanohydrolase h(a16-M).
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Authors
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M.Hahn,
T.Keitel,
U.Heinemann.
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Ref.
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Eur J Biochem, 1995,
232,
849-858.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
89%.
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Abstract
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H(A16-M) is a hybrid endo-1,3-1,4-beta-D-glucan 4-glucanohydrolase from
Bacillus. Its crystal structure was refined using synchrotron X-ray diffraction
data up to a maximal resolution of 0.16 nm. The R value of the resulting model
is 14.3% against 21,032 reflections > 2 sigma. 93% of the amino acid residues
are in the most favorable regions of the Ramachandran diagram, and geometrical
parameters are in accordance with other proteins solved at high resolution. As
shown earlier [Keitel, T., Simon, O., Borriss, R. & Heinemann, U. (1993)
Proc. Natl Acad. Sci. USA 90, 5287-5291], the protein folds into a compact
jellyroll-type beta-sheet structure. A systematic analysis of the secondary
structure reveals the presence of two major antiparallel beta-sheets and a
three-stranded minor mixed sheet. Amino acid residues involved in catalysis and
substrate binding are located inside a deep channel spanning the surface of the
protein. To investigate the stereochemical cause of the observed specificity of
endo-1,3-1,4-beta-D-glucan 4-glucanohydrolases towards beta-1,4 glycosyl bonds
adjacent to beta-1,3 bonds, the high-resolution crystal structure has been used
to model an enzyme-substrate complex. It is proposed that productive substrate
binding to the subsites p1, p2 and p3 of H(A16-M) requires a beta-1,3 linkage
between glucose units bound to p1 and p2.
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Secondary reference #1
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Title
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Molecular and active-Site structure of a bacillus 1,3-1,4-Beta-Glucanase.
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Authors
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T.Keitel,
O.Simon,
R.Borriss,
U.Heinemann.
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Ref.
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Proc Natl Acad Sci U S A, 1993,
90,
5287-5291.
[DOI no: ]
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PubMed id
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