2pec
From Proteopedia
(New page: 200px<br /><applet load="2pec" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pec, resolution 2.2Å" /> '''THE REFINED THREE-DIM...) |
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| - | [[Image:2pec.gif|left|200px]]<br /><applet load="2pec" size=" | + | [[Image:2pec.gif|left|200px]]<br /><applet load="2pec" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2pec, resolution 2.2Å" /> | caption="2pec, resolution 2.2Å" /> | ||
'''THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM'''<br /> | '''THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM'''<br /> | ||
==Overview== | ==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 | + | 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== | ==About this Structure== | ||
| - | 2PEC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. This structure | + | 2PEC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. This structure supersedes the now removed PDB entry 1PEC. 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=2PEC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Jurnak, F.]] | [[Category: Jurnak, F.]] | ||
| - | [[Category: Yoder, M | + | [[Category: Yoder, M D.]] |
[[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 18:28:36 2008'' |
Revision as of 16:28, 21 February 2008
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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
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. Active as Pectate lyase, with EC number 4.2.2.2 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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