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.


1so0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1so0.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1so0.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1so0| PDB=1so0 | SCENE= }}
{{STRUCTURE_1so0| PDB=1so0 | SCENE= }}
-
'''Crystal structure of human galactose mutarotase complexed with galactose'''
+
===Crystal structure of human galactose mutarotase complexed with galactose===
-
==Overview==
+
<!--
-
Galactose mutarotase catalyzes the conversion of beta-d-galactose to alpha-d-galactose during normal galactose metabolism. The enzyme has been isolated from bacteria, plants, and animals and is present in the cytoplasm of most cells. Here we report the x-ray crystallographic analysis of human galactose mutarotase both in the apoform and complexed with its substrate, beta-d-galactose. The polypeptide chain folds into an intricate array of 29 beta-strands, 25 classical reverse turns, and 2 small alpha-helices. There are two cis-peptide bonds at Arg-78 and Pro-103. The sugar ligand sits in a shallow cleft and is surrounded by Asn-81, Arg-82, His-107, His-176, Asp-243, Gln-279, and Glu-307. Both the side chains of Glu-307 and His-176 are in the proper location to act as a catalytic base and a catalytic acid, respectively. These residues are absolutely conserved among galactose mutarotases. To date, x-ray models for three mutarotases have now been reported, namely that described here and those from Lactococcus lactis and Caenorhabditis elegans. The molecular architectures of these enzymes differ primarily in the loop regions connecting the first two beta-strands. In the human protein, there are six extra residues in the loop compared with the bacterial protein for an approximate longer length of 9 A. In the C. elegans protein, the first 17 residues are missing, thereby reducing the total number of beta-strands by one.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15026423}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15026423 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15026423}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Galactosemia]]
[[Category: Galactosemia]]
[[Category: Mutartoase]]
[[Category: Mutartoase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:56:24 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:44:33 2008''

Revision as of 12:44, 29 July 2008

Image:1so0.png

Template:STRUCTURE 1so0

Crystal structure of human galactose mutarotase complexed with galactose

Template:ABSTRACT PUBMED 15026423

About this Structure

1SO0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Molecular structure of human galactose mutarotase., Thoden JB, Timson DJ, Reece RJ, Holden HM, J Biol Chem. 2004 May 28;279(22):23431-7. Epub 2004 Mar 16. PMID:15026423

Page seeded by OCA on Tue Jul 29 15:44:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1so0"
Personal tools