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.


1ma0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ma0.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1ma0.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ma0| PDB=1ma0 | SCENE= }}
{{STRUCTURE_1ma0| PDB=1ma0 | SCENE= }}
-
'''Ternary complex of Human glutathione-dependent formaldehyde dehydrogenase with NAD+ and dodecanoic acid'''
+
===Ternary complex of Human glutathione-dependent formaldehyde dehydrogenase with NAD+ and dodecanoic acid===
-
==Overview==
+
<!--
-
The human glutathione-dependent formaldehyde dehydrogenase is unique among the structurally studied members of the alcohol dehydrogenase family in that it follows a random bi bi kinetic mechanism. The structures of an apo form of the enzyme, a binary complex with substrate 12-hydroxydodecanoic acid, and a ternary complex with NAD+ and the inhibitor dodecanoic acid were determined at 2.0, 2.3, and 2.3 A resolution by X-ray crystallography using the anomalous diffraction signal of zinc. The structures of the enzyme and its binary complex with the primary alcohol substrate, 12-hydroxydodecanoic acid, and the previously reported binary complex with the coenzyme show that the binding of the first substrate (alcohol or coenzyme) causes only minor changes to the overall structure of the enzyme. This is consistent with the random mechanism of the enzyme where either of the substrates binds to the free enzyme. The catalytic-domain position in these structures is intermediate to the "closed" and "open" conformations observed in class I alcohol dehydrogenases. More importantly, two different tetrahedral coordination environments of the active site zinc are observed in these structures. In the apoenzyme, the active site zinc is coordinated to Cys44, His66 and Cys173, and a water molecule. In the inhibitor complex, the coordination environment involves Glu67 instead of the solvent water molecule. The coordination environment involving Glu67 as the fourth ligand likely represents an intermediate step during ligand exchange at the active site zinc. These observations provide new insight into metal-assisted catalysis and substrate binding in glutathione-dependent formaldehyde dehydrogenase.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12196016}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12196016 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12196016}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Class iii alcohol dehydrogenase]]
[[Category: Class iii alcohol dehydrogenase]]
[[Category: Human glutathione-dependent formaldehyde dehydrogenase]]
[[Category: Human glutathione-dependent formaldehyde dehydrogenase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:48:40 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:31:43 2008''

Revision as of 20:31, 2 July 2008

Image:1ma0.png

Template:STRUCTURE 1ma0

Ternary complex of Human glutathione-dependent formaldehyde dehydrogenase with NAD+ and dodecanoic acid

Template:ABSTRACT PUBMED 12196016

About this Structure

1MA0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Human glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes., Sanghani PC, Robinson H, Bosron WF, Hurley TD, Biochemistry. 2002 Sep 3;41(35):10778-86. PMID:12196016

Page seeded by OCA on Wed Jul 2 23:31:43 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ma0"
Personal tools