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* Residue conservation analysis
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Enzyme class:
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Chains A, B:
E.C.3.2.1.73
- Licheninase.
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Reaction:
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Hydrolysis of 1,4-beta-D-glycosidic linkages in beta-D-glucans containing 1,3- and 1,4-bonds.
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Gene Ontology (GO) functional annotation
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Biological process
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metabolic process
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2 terms
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Biochemical function
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hydrolase activity
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4 terms
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DOI no:
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Proteins
30:155-167
(1998)
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PubMed id:
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Crystal structures and properties of de novo circularly permuted 1,3-1,4-beta-glucanases.
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J.Aÿ,
M.Hahn,
K.Decanniere,
K.Piotukh,
R.Borriss,
U.Heinemann.
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ABSTRACT
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The 1,3-1,4-beta-glucanases from Bacillus macerans and Bacillus licheniformis,
as well as related hybrid enzymes, are stable proteins comprised of one compact
jellyroll domain. Their structures are studied in an effort to reveal the degree
of redundancy to which the three-dimensional structure of protein domains is
encoded by the amino acid sequence. For the hybrid 1,3-1,4-beta-glucanase
H(A16-M), it could be shown recently that a circular permutation of the sequence
giving rise to the variant cpA16M-59 is compatible with wildtype-like enzymatic
activity and tertiary structure (Hahn et al., Proc. Natl. Acad. Sci. USA
91:10417-10421, 1994). Since the circular permutation yielding cpA16M-59 mimicks
that found in the homologous enzyme from Fibrobacter succinogenes, the question
arose whether de novo circular permutations, not guided by molecular evolution
of the 1,3-1,4-beta-glucanases, could also produce proteins with native-like
fold. The circularly permuted variants cpA16M-84, cpA16M-127, and cpA16M-154
were generated by PCR mutagenesis of the gene encoding H(A16-M), synthesized in
Escherichia coli and shown to be active in beta-glucan hydrolysis. CpA16M-84 and
cpA16M-127 were crystallized in space groups P2(1) and P1, respectively, and
their crystal structures were determined at 1.80 and 2.07 A resolution. In both
proteins the main parts of the beta-sheet structure remain unaffected by the
circular permutation as is evident from a root-mean-square deviation of main
chain atoms from the reference structure within the experimental error. The only
major structural perturbation occurs near the novel chain termini in a surface
loop of cpA16M-84, which becomes destabilized and rearranged. The results of
this study are interpreted to show that: (1) several circular permutations in
the compact jellyroll domain of the 1,3-1,4-beta-glucanases are tolerated
without radical change of enzymatic activity or tertiary structure, (2) the
three-dimensional structures of simple domains are encoded by the amino acid
sequence with sufficient redundancy to tolerate a change in the sequential order
of secondary structure elements along the sequence, and (3) the native
N-terminal region is not needed to guide the folding polypeptide chain toward
its native conformation.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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Z.Qian,
J.R.Horton,
X.Cheng,
and
S.Lutz
(2009).
Structural redesign of lipase B from Candida antarctica by circular permutation and incremental truncation.
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J Mol Biol, 393,
191-201.
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PDB codes:
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A.M.Lisewski
(2008).
Random amino acid mutations and protein misfolding lead to Shannon limit in sequence-structure communication.
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PLoS ONE, 3,
e3110.
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A.Abyzov,
and
V.A.Ilyin
(2007).
A comprehensive analysis of non-sequential alignments between all protein structures.
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BMC Struct Biol, 7,
78.
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G.Fibriansah,
S.Masuda,
N.Koizumi,
S.Nakamura,
and
T.Kumasaka
(2007).
The 1.3 A crystal structure of a novel endo-beta-1,3-glucanase of glycoside hydrolase family 16 from alkaliphilic Nocardiopsis sp. strain F96.
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Proteins, 69,
683-690.
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PDB code:
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B.A.Manjasetty,
J.Hennecke,
R.Glockshuber,
and
U.Heinemann
(2004).
Structure of circularly permuted DsbA(Q100T99): preserved global fold and local structural adjustments.
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Acta Crystallogr D Biol Crystallogr, 60,
304-309.
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PDB code:
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T.U.Schwartz,
R.Walczak,
and
G.Blobel
(2004).
Circular permutation as a tool to reduce surface entropy triggers crystallization of the signal recognition particle receptor beta subunit.
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Protein Sci, 13,
2814-2818.
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V.F.Smith,
and
C.R.Matthews
(2001).
Testing the role of chain connectivity on the stability and structure of dihydrofolate reductase from E. coli: fragment complementation and circular permutation reveal stable, alternatively folded forms.
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Protein Sci, 10,
116-128.
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A.Planas
(2000).
Bacterial 1,3-1,4-beta-glucanases: structure, function and protein engineering.
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Biochim Biophys Acta, 1543,
361-382.
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L.Regan
(1999).
Protein redesign.
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Curr Opin Struct Biol, 9,
494-499.
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S.Gleiter,
K.Stubenrauch,
and
H.Lilie
(1999).
Changing the surface of a virus shell fusion of an enzyme to polyoma VP1.
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Protein Sci, 8,
2562-2569.
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J.Aÿ,
F.Götz,
R.Borriss,
and
U.Heinemann
(1998).
Structure and function of the Bacillus hybrid enzyme GluXyn-1: native-like jellyroll fold preserved after insertion of autonomous globular domain.
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Proc Natl Acad Sci U S A, 95,
6613-6618.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
