We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1vd5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vd5.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1vd5.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1vd5| PDB=1vd5 | SCENE= }}
{{STRUCTURE_1vd5| PDB=1vd5 | SCENE= }}
-
'''Crystal Structure of Unsaturated Glucuronyl Hydrolase, Responsible for the Degradation of Glycosaminoglycan, from Bacillus sp. GL1 at 1.8 A Resolution'''
+
===Crystal Structure of Unsaturated Glucuronyl Hydrolase, Responsible for the Degradation of Glycosaminoglycan, from Bacillus sp. GL1 at 1.8 A Resolution===
-
==Overview==
+
<!--
-
Unsaturated glucuronyl hydrolase (UGL) is a novel glycosaminoglycan hydrolase that releases unsaturated d-glucuronic acid from oligosaccharides produced by polysaccharide lyases. The x-ray crystallographic structure of UGL from Bacillus sp. GL1 was first determined by multiple isomorphous replacement (mir) and refined at 1.8 A resolution with a final R-factor of 16.8% for 25 to 1.8 A resolution data. The refined UGL structure consists of 377 amino acid residues and 478 water molecules, four glycine molecules, two dithiothreitol (DTT) molecules, and one 2-methyl-2,4-pentanediol (MPD) molecule. UGL includes an alpha(6)/alpha(6)-barrel, whose structure is found in the six-hairpin enzyme superfamily of an alpha/alpha-toroidal fold. One side of the UGL alpha(6)/alpha(6)-barrel structure consists of long loops containing three short beta-sheets and contributes to the formation of a deep pocket. One glycine molecule and two DTT molecules surrounded by highly conserved amino acid residues in UGLs were found in the pocket, suggesting that catalytic and substrate-binding sites are located in this pocket. The overall UGL structure, with the exception of some loops, very much resembled that of the Bacillus subtilis hypothetical protein Yter, whose function is unknown and which exhibits little amino acid sequence identity with UGL. In the active pocket, residues possibly involved in substrate recognition and catalysis by UGL are conserved in UGLs and Yter. The most likely candidate catalytic residues for glycosyl hydrolysis are Asp(88) and Asp(149). This was supported by site-directed mutagenesis studies in Asp(88) and Asp(149).
+
The line below this paragraph, {{ABSTRACT_PUBMED_15148314}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15148314 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15148314}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Alpha-alpha-barrel]]
[[Category: Alpha-alpha-barrel]]
[[Category: Unsaturated glucuronyl hydrolase]]
[[Category: Unsaturated glucuronyl hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:23:56 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:48:23 2008''

Revision as of 10:48, 28 July 2008

Image:1vd5.png

Template:STRUCTURE 1vd5

Crystal Structure of Unsaturated Glucuronyl Hydrolase, Responsible for the Degradation of Glycosaminoglycan, from Bacillus sp. GL1 at 1.8 A Resolution

Template:ABSTRACT PUBMED 15148314

About this Structure

1VD5 is a Single protein structure of sequence from Bacillus sp.. Full crystallographic information is available from OCA.

Reference

Crystal structure of unsaturated glucuronyl hydrolase, responsible for the degradation of glycosaminoglycan, from Bacillus sp. GL1 at 1.8 A resolution., Itoh T, Akao S, Hashimoto W, Mikami B, Murata K, J Biol Chem. 2004 Jul 23;279(30):31804-12. Epub 2004 May 17. PMID:15148314

Page seeded by OCA on Mon Jul 28 13:48:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vd5"
Personal tools