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.


2fuc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2fuc.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2fuc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2fuc| PDB=2fuc | SCENE= }}
{{STRUCTURE_2fuc| PDB=2fuc | SCENE= }}
-
'''Human alpha-Phosphomannomutase 1 with Mg2+ cofactor bound'''
+
===Human alpha-Phosphomannomutase 1 with Mg2+ cofactor bound===
-
==Overview==
+
<!--
-
Congenital disorder of glycosylation type 1a (CDG-1a) is a congenital disease characterized by severe defects in nervous system development. It is caused by mutations in alpha-phosphomannomutase (of which there are two isozymes, alpha-PMM1 and alpha-PPM2). Here we report the x-ray crystal structures of human alpha-PMM1 in the open conformation, with and without the bound substrate, alpha-D-mannose 1-phosphate. Alpha-PMM1, like most haloalkanoic acid dehalogenase superfamily (HADSF) members, consists of two domains, the cap and core, which open to bind substrate and then close to provide a solvent-exclusive environment for catalysis. The substrate phosphate group is observed at a positively charged site of the cap domain, rather than at the core domain phosphoryl-transfer site defined by the Asp(19) nucleophile and Mg(2+) cofactor. This suggests that substrate binds first to the cap and then is swept into the active site upon cap closure. The orientation of the acid/base residue Asp(21) suggests that alpha-phosphomannomutase (alpha-PMM) uses a different method of protecting the aspartylphosphate from hydrolysis than the HADSF member beta-phosphoglucomutase. It is hypothesized that the electrostatic repulsion of positive charges at the interface of the cap and core domains stabilizes alpha-PMM1 in the open conformation and that the negatively charged substrate binds to the cap, thereby facilitating its closure over the core domain. The two isozymes, alpha-PMM1 and alpha-PMM2, are shown to have a conserved active-site structure and to display similar kinetic properties. Analysis of the known mutation sites in the context of the structures reveals the genotype-phenotype relationship underlying CDG-1a.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16540464}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16540464 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16540464}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Phosphomannomutase]]
[[Category: Phosphomannomutase]]
[[Category: Protein glycosylation]]
[[Category: Protein glycosylation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:19:06 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:44:41 2008''

Revision as of 09:44, 27 July 2008

Image:2fuc.png

Template:STRUCTURE 2fuc

Human alpha-Phosphomannomutase 1 with Mg2+ cofactor bound

Template:ABSTRACT PUBMED 16540464

About this Structure

2FUC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a., Silvaggi NR, Zhang C, Lu Z, Dai J, Dunaway-Mariano D, Allen KN, J Biol Chem. 2006 May 26;281(21):14918-26. Epub 2006 Mar 15. PMID:16540464

Page seeded by OCA on Sun Jul 27 12:44:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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