1pcl
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= PPEL748 OF PELC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=556 Erwinia chrysanthemi]) | |GENE= PPEL748 OF PELC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=556 Erwinia chrysanthemi]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pcl OCA], [http://www.ebi.ac.uk/pdbsum/1pcl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pcl RCSB]</span> | ||
}} | }} | ||
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[[Category: lyase (acting on polysaccharides)]] | [[Category: lyase (acting on polysaccharides)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:57:53 2008'' |
Revision as of 19:57, 30 March 2008
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| , resolution 2.2Å | |||||||
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| Gene: | PPEL748 OF PELC (Erwinia chrysanthemi) | ||||||
| Activity: | Pectate lyase, with EC number 4.2.2.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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