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.


1hn0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hn0.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1hn0.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hn0| PDB=1hn0 | SCENE= }}
{{STRUCTURE_1hn0| PDB=1hn0 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION'''
+
===CRYSTAL STRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION===
-
==Overview==
+
<!--
-
Chondroitin Sulfate ABC lyase I from Proteus vulgaris is an endolytic, broad-specificity glycosaminoglycan lyase, which degrades chondroitin, chondroitin-4-sulfate, dermatan sulfate, chondroitin-6-sulfate, and hyaluronan by beta-elimination of 1,4-hexosaminidic bond to unsaturated disaccharides and tetrasaccharides. Its structure revealed three domains. The N-terminal domain has a fold similar to that of carbohydrate-binding domains of xylanases and some lectins, the middle and C-terminal domains are similar to the structures of the two-domain chondroitin lyase AC and bacterial hyaluronidases. Although the middle domain shows a very low level of sequence identity with the catalytic domains of chondroitinase AC and hyaluronidase, the residues implicated in catalysis of the latter enzymes are present in chondroitinase ABC I. The substrate-binding site in chondroitinase ABC I is in a wide-open cleft, consistent with the endolytic action pattern of this enzyme. The tryptophan residues crucial for substrate binding in chondroitinase AC and hyaluronidases are lacking in chondroitinase ABC I. The structure of chondroitinase ABC I provides a framework for probing specific functions of active-site residues for understanding the remarkably broad specificity of this enzyme and perhaps engineering a desired specificity. The electron density map showed clearly that the deposited DNA sequence for residues 495-530 of chondroitin ABC lyase I, the segment containing two putative active-site residues, contains a frame-shift error resulting in an incorrectly translated amino acid sequence.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12706721}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12706721 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12706721}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Chonroitin digestion]]
[[Category: Chonroitin digestion]]
[[Category: Mechanism]]
[[Category: Mechanism]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:01:40 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:25:00 2008''

Revision as of 05:25, 1 July 2008

Image:1hn0.png

Template:STRUCTURE 1hn0

CRYSTAL STRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 12706721

About this Structure

1HN0 is a Single protein structure of sequence from Proteus vulgaris. Full crystallographic information is available from OCA.

Reference

Crystal structure of Proteus vulgaris chondroitin sulfate ABC lyase I at 1.9A resolution., Huang W, Lunin VV, Li Y, Suzuki S, Sugiura N, Miyazono H, Cygler M, J Mol Biol. 2003 May 2;328(3):623-34. PMID:12706721

Page seeded by OCA on Tue Jul 1 08:25:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hn0"
Personal tools