This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2baa

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2baa.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2baa.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2baa| PDB=2baa | SCENE= }}
{{STRUCTURE_2baa| PDB=2baa | SCENE= }}
-
'''THE REFINED CRYSTAL STRUCTURE OF AN ENDOCHITINASE FROM HORDEUM VULGARE L. SEEDS TO 1.8 ANGSTROMS RESOLUTION'''
+
===THE REFINED CRYSTAL STRUCTURE OF AN ENDOCHITINASE FROM HORDEUM VULGARE L. SEEDS TO 1.8 ANGSTROMS RESOLUTION===
-
==Overview==
+
<!--
-
Class II chitinases (EC 3.2.1.14) are plant defense proteins. They hydrolyze chitin, an insoluble beta-1,4-linked polymer of N-acetylglucosamine (NAG), which is a major cell-wall component of many fungal hyphae. We previously reported the three-dimensional structure of the 26 kDa class II endochitinase from barley seeds at 2.8 A resolution, determined using multiple isomorphous replacement (MIR) methods. Here, we report the crystallographic refinement of this chitinase structure against data to 1.8 A resolution using rounds of hand rebuilding coupled with molecular dynamics (X-PLOR). The final model has an R-value of 18.1% for the 5.0 to 1.8 A data shell and 19.8% for the 10.0 to 1.8 A shell, and root-mean-square deviations from standard bond lengths and angles of 0.017 A and 2.88 degrees, respectively. The 243 residue molecule has one beta-sheet, ten alpha-helices and three disulfide bonds; 129 water molecules are included in the final model. We show structural comparisons confirming that chitinase secondary structure resembles lysozyme at the active site region. Based on substrate binding to lysozyme, we have built a hypothetical model for the binding of a hexasaccharide into the pronounced active site cleft of chitinase. This provides the first view of likely substrate interactions from this family of enzymes; the model is consistent with a lysozyme-like mechanism of action in which Glu67 acts as proton donor and Glu89 is likely to stabilize the transition state oxycarbonium ion. These binding site residues, and many hydrophobic residues are conserved in a range of plant chitinases. This endochitinase structure will serve as a model for other plant chitinases, and that catalytic models based on this structure will be applicable to the entire enzyme family.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7739049}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7739049 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7739049}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Ready, M P.]]
[[Category: Ready, M P.]]
[[Category: Robertus, J D.]]
[[Category: Robertus, J D.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:02:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:16:43 2008''

Revision as of 13:16, 28 July 2008

Image:2baa.png

Template:STRUCTURE 2baa

THE REFINED CRYSTAL STRUCTURE OF AN ENDOCHITINASE FROM HORDEUM VULGARE L. SEEDS TO 1.8 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 7739049

About this Structure

2BAA is a Single protein structure of sequence from Hordeum vulgare. This structure supersedes the now removed PDB entry 1baa. Full crystallographic information is available from OCA.

Reference

The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8 A resolution., Hart PJ, Pfluger HD, Monzingo AF, Hollis T, Robertus JD, J Mol Biol. 1995 Apr 28;248(2):402-13. PMID:7739049

Page seeded by OCA on Mon Jul 28 16:16:43 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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