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.


2qly

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2qly.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2qly.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2qly| PDB=2qly | SCENE= }}
{{STRUCTURE_2qly| PDB=2qly | SCENE= }}
-
'''Crystral Structure of the N-terminal Subunit of Human Maltase-Glucoamylase'''
+
===Crystral Structure of the N-terminal Subunit of Human Maltase-Glucoamylase===
-
==Overview==
+
<!--
-
Human maltase-glucoamylase (MGAM) is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM). In this study, we report the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A). Structural analysis of the NtMGAM-acarbose complex reveals that acarbose is bound to the NtMGAM active site primarily through side-chain interactions with its acarvosine unit, and almost no interactions are made with its glycone rings. These observations, along with results from kinetic studies, suggest that the NtMGAM active site contains two primary sugar subsites and that NtMGAM and CtMGAM differ in their substrate specificities despite their structural relationship. Additional sequence analysis of the CtMGAM subunit suggests several features that could explain the higher affinity of the CtMGAM subunit for longer maltose oligosaccharides. The results provide a structural basis for the complementary roles of these glycosyl hydrolase family 31 subunits in the bioprocessing of complex starch structures into glucose.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18036614}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18036614 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18036614}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Sulfation]]
[[Category: Sulfation]]
[[Category: Transmembrane]]
[[Category: Transmembrane]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:10:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:03:58 2008''

Revision as of 03:04, 28 July 2008

Image:2qly.png

Template:STRUCTURE 2qly

Crystral Structure of the N-terminal Subunit of Human Maltase-Glucoamylase

Template:ABSTRACT PUBMED 18036614

About this Structure

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

Reference

Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity., Sim L, Quezada-Calvillo R, Sterchi EE, Nichols BL, Rose DR, J Mol Biol. 2008 Jan 18;375(3):782-92. Epub 2007 Nov 1. PMID:18036614

Page seeded by OCA on Mon Jul 28 06:03:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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