1pcl
From Proteopedia
(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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| - | [[Image:1pcl.gif|left|200px]]<br /><applet load="1pcl" size=" | + | [[Image:1pcl.gif|left|200px]]<br /><applet load="1pcl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pcl, resolution 2.2Å" /> | caption="1pcl, resolution 2.2Å" /> | ||
'''UNUSUAL STRUCTURAL FEATURES IN THE PARALLEL BETA-HELIX IN PECTATE LYASES'''<br /> | '''UNUSUAL STRUCTURAL FEATURES IN THE PARALLEL BETA-HELIX IN PECTATE LYASES'''<br /> | ||
==Overview== | ==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 | + | 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== | ==About this Structure== | ||
| - | 1PCL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. Active as [http://en.wikipedia.org/wiki/Pectate_lyase Pectate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.2 4.2.2.2] Full crystallographic information is available from [http:// | + | 1PCL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. Active as [http://en.wikipedia.org/wiki/Pectate_lyase Pectate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.2 4.2.2.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Jurnak, F.]] | [[Category: Jurnak, F.]] | ||
| - | [[Category: Keen, N | + | [[Category: Keen, N T.]] |
| - | [[Category: Lietzke, S | + | [[Category: Lietzke, S E.]] |
[[Category: lyase (acting on polysaccharides)]] | [[Category: lyase (acting on polysaccharides)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:24 2008'' |
Revision as of 12:27, 21 February 2008
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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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