2pec
From Proteopedia
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| - | [[Image:2pec.gif|left|200px]] | + | [[Image:2pec.gif|left|200px]] |
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| - | '''THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM''' | + | {{Structure |
| + | |PDB= 2pec |SIZE=350|CAPTION= <scene name='initialview01'>2pec</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |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] | ||
| + | |GENE= PPEL410 OF PELC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=556 Erwinia chrysanthemi]) | ||
| + | }} | ||
| + | |||
| + | '''THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2PEC is a [ | + | 2PEC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. This structure supersedes the now removed PDB entry 1PEC. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PEC OCA]. |
==Reference== | ==Reference== | ||
| - | Protein motifs. 3. The parallel beta helix and other coiled folds., Yoder MD, Jurnak F, FASEB J. 1995 Mar;9(5):335-42. PMID:[http:// | + | Protein motifs. 3. The parallel beta helix and other coiled folds., Yoder MD, Jurnak F, FASEB J. 1995 Mar;9(5):335-42. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7896002 7896002] |
[[Category: Erwinia chrysanthemi]] | [[Category: Erwinia chrysanthemi]] | ||
[[Category: Pectate lyase]] | [[Category: Pectate lyase]] | ||
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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 Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:11:56 2008'' |
Revision as of 16:11, 20 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | PPEL410 OF PELC (Erwinia chrysanthemi) | ||||||
| Activity: | Pectate lyase, with EC number 4.2.2.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM
Overview
A new type of structural domain, composed of all parallel beta strands, has been observed within the last year. An analysis of the basic types suggests that there are two distinct classes: the parallel beta helices, which belong to a tri beta-strand category, and the beta roll, which belongs to a di beta-strand category. The novel structural features of each class are described and the proteins belonging to each category are summarized. Proteins with the parallel beta helix fold include three pectate lyases and the tailspike protein from P22 phage. Proteins with the beta roll fold include two alkaline proteases. Although the parallel beta composition is emphasized, the same set of proteins share another common structural feature with several other proteins containing alpha helices: the polypeptide backbone is folded into a coiled structure in which each coil has the same 3-dimensional arrangement of a group of secondary structural elements. In addition to parallel beta domains, the other groups include the alpha/beta coiled fold, as represented by ribonuclease inhibitor, and the alpha/alpha coiled fold, as represented by lipovitellin and soluble lytic transglycoslyase. Novel features of the alpha/beta and alpha/alpha coiled folds are summarized.
About this Structure
2PEC is a Single protein structure of sequence from Erwinia chrysanthemi. This structure supersedes the now removed PDB entry 1PEC. Full crystallographic information is available from OCA.
Reference
Protein motifs. 3. The parallel beta helix and other coiled folds., Yoder MD, Jurnak F, FASEB J. 1995 Mar;9(5):335-42. PMID:7896002
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