1pcl
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(New page: 200px<br /><applet load="1pcl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pcl, resolution 2.2Å" /> '''UNUSUAL STRUCTURAL FE...)
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Revision as of 21:34, 20 November 2007
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UNUSUAL STRUCTURAL FEATURES IN THE PARALLEL BETA-HELIX IN PECTATE LYASES
Overview
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.
About this Structure
1PCL is a Single protein structure of sequence from Erwinia chrysanthemi. Active as Pectate lyase, with EC number 4.2.2.2 Full crystallographic information is available from OCA.
Reference
Unusual structural features in the parallel beta-helix in pectate lyases., Yoder MD, Lietzke SE, Jurnak F, Structure. 1993 Dec 15;1(4):241-51. PMID:8081738
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