2pec

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2pec.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2pec.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2pec| PDB=2pec | SCENE= }}
{{STRUCTURE_2pec| PDB=2pec | SCENE= }}
-
'''THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7896002}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7896002 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7896002}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Jurnak, F.]]
[[Category: Jurnak, F.]]
[[Category: Yoder, M D.]]
[[Category: Yoder, M D.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:57:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:19:43 2008''

Revision as of 17:19, 27 July 2008

Image:2pec.png

Template:STRUCTURE 2pec

THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM

Template:ABSTRACT PUBMED 7896002

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

Page seeded by OCA on Sun Jul 27 20:19:43 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pec"
Personal tools