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PDBsum entry 1pcl
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Lyase (acting on polysaccharides)
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PDB id
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1pcl
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References listed in PDB file
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Key reference
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Title
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Unusual structural features in the parallel beta-Helix in pectate lyases.
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Authors
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M.D.Yoder,
S.E.Lietzke,
F.Jurnak.
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Ref.
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Structure, 1993,
1,
241-251.
[DOI no: ]
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PubMed id
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Abstract
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BACKGROUND: A new type of domain structure, an all parallel beta class, has
recently been observed in two pectate lyases, PelC and PelE. The atomic models
have been analyzed to determine whether the new tertiary fold exhibits unusual
structural features. RESULTS: The polypeptide backbone exhibits no new types of
secondary structural elements. However, novel features occur in the amino acid
side chain interactions. The side chain atoms form linear stacks that include
asparagine ladders, serine stacks, aliphatic stacks, and ringed-residue stacks.
A new type of beta-sandwich between parallel beta-sheets is observed with
properties that are more characteristic of antiparallel beta-sheets. CONCLUSION:
An analysis of the PelC and PelE structures, belonging to an all parallel beta
structural class, reveals novel amino acid side chain interactions, a new type
of beta-sandwich and an atypical amino acid composition of parallel beta-sheets.
The findings are relevant to three-dimensional structural predictions.
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Figure 1.
Fig. 1. Schematics of PelC and PelE. Ribbon iagram of (a) PelC and (b) PelE. Arrows represent ~-structure, and coils represent e~-helices.
Each of the three parallel sheets is depicted in a different color, PB2 is ingree, PB1 in yelow and PB3 in red. (c) The superposition of
the core regions f PelE on PelC. Loops extending out from the core region are xcluded. Th PeIC C~ chain trace is in yellow and the
PelE Cc~ chain trace is in blue.
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Figure 7.
Fig. 7. The hydrogen bonding pattern
of the asparagine ladder. Three
aspargine residues of the asparagine
ladder in PeIC. (b) Three residues of
the asparagine ladder in PelE, includ'-
ing Ser307. The Cc~ chain trace is in
gray. Carbon atoms are lack; itrogen
atoms, dark ray; oxygen atoms, gray;
and hydrogen atoms, white. Hydrogen
bons are indicated by dashed lines.
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The above figures are
reprinted
by permission from Cell Press:
Structure
(1993,
1,
241-251)
copyright 1993.
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Secondary reference #1
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Title
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The refined three-Dimensional structure of pectate lyase e from erwinia chrysanthemi at 2.2 a resolution.
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Authors
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S.E.Lietzke,
R.D.Scavetta,
M.D.Yoder,
F.Jurnak.
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Ref.
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Plant Physiol, 1996,
111,
73-92.
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PubMed id
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Secondary reference #2
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Title
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Preliminary crystallographic analysis of a plant pathogenic factor: pectate lyase.
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Authors
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C.Y.Kim,
V.Mosser,
N.Keen,
F.Jurnak.
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Ref.
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J Mol Biol, 1989,
208,
365-367.
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PubMed id
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Secondary reference #3
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Title
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Structure of two pectate lyase genes from erwinia chrysanthemi ec16 and their high-Level expression in escherichia coli.
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Authors
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N.T.Keen,
S.Tamaki.
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Ref.
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J Bacteriol, 1986,
168,
595-606.
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PubMed id
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Headers
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