3hud

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:3hud.jpg|left|200px]]
[[Image:3hud.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 3hud |SIZE=350|CAPTION= <scene name='initialview01'>3hud</scene>, resolution 3.2&Aring;
+
The line below this paragraph, containing "STRUCTURE_3hud", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_3hud| PDB=3hud | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3hud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hud OCA], [http://www.ebi.ac.uk/pdbsum/3hud PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3hud RCSB]</span>
+
-
}}
+
'''THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS'''
'''THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS'''
Line 30: Line 27:
[[Category: Hamilton, J A.]]
[[Category: Hamilton, J A.]]
[[Category: Hurley, T D.]]
[[Category: Hurley, T D.]]
-
[[Category: oxidoreductase(nad(a)-choh(d))]]
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:04:24 2008''
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:33:58 2008''
+

Revision as of 19:04, 4 May 2008

Image:3hud.jpg

Template:STRUCTURE 3hud

THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS


Overview

The three-dimensional structure of human beta 1 beta 1 alcohol dehydrogenase (ADH; EC 1.1.1.1) complexed with NAD+ has been determined by x-ray crystallography to 3.0-A resolution. The amino acids directly involved in coenzyme binding are conserved between horse EE and human beta 1 beta 1 alcohol dehydrogenase in all but one case [serine (horse) vs. threonine (human) at position 48]. As a result, the coenzyme molecule is bound in a similar manner in the two enzymes. However, the strength of the interactions in the vicinity of the pyrophosphate bridge of NAD+ appears to be enhanced in the human enzyme. Side-chain movements of Arg-47 and Asp-50 and a shift in the position of the helix comprising residues 202-212 may explain both the decreased Vmax and the decreased rate of NADH dissociation observed in the human enzyme vs. the horse enzyme. It appears that these catalytic differences are not due to substitutions of any amino acids directly involved in coenzyme binding but are the result of structural rearrangements resulting from multiple sequence differences between the two enzymes.

About this Structure

3HUD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions., Hurley TD, Bosron WF, Hamilton JA, Amzel LM, Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8149-53. PMID:1896463 Page seeded by OCA on Sun May 4 22:04:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3hud"
Personal tools