2zea: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px <!-- The line below this paragraph, containing "STRUCTURE_2zea", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:2zea.jpg|left|200px]]
{{Seed}}
[[Image:2zea.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2zea|  PDB=2zea  |  SCENE=  }}  
{{STRUCTURE_2zea|  PDB=2zea  |  SCENE=  }}  


'''Crystal structure of Alcaligenes faecalis D-3-hydroxybutyrate dehydrogenase in complex with NAD+ and acetate'''
===Crystal structure of Alcaligenes faecalis D-3-hydroxybutyrate dehydrogenase in complex with NAD+ and acetate===




==Overview==
<!--  
D-3-Hydroxybutyrate dehydrogenase, which catalyzes the reversible reaction between D-3-hydroxybutyrate and acetoacetate, has been classified into the short-chain dehydrogenase/reductase family and is a useful marker in the assay of diabetes mellitus and/or ketoacidosis. The enzyme from Alcaligenes faecalis was crystallized in the apo form and in the holo form with acetate as a substrate analogue. The crystal structures of both forms were determined at 2.2 angstroms resolution. The enzyme is a tetramer composed of four subunits assembled with noncrystallographic 222 point symmetry. Each subunit has two domains. The principal domain adopts the Rossmann fold essential for nucleotide binding, which is a common feature of the SDR family. NAD+ is bound in a large cleft in the domain. The pyrophosphate group of NAD+ is covered by the small additional domain, which is supported by two extended arms allowing domain movement. In the catalytic site, a water molecule is trapped by the catalytic Tyr155 and Ser142 residues in the vicinity of the bound NAD+ and acetate. The substrate analogue acetate is bound above the nicotinamide plane. A substrate (D-3-hydroxybutylate) bound model can reasonably be constructed by adding two C atoms into the void space between the water O atom and the methyl group of the acetate, suggesting a substrate-bound state before enzymatic reaction occurs. Based on these structural features, a reaction mechanism has been proposed.
The line below this paragraph, {{ABSTRACT_PUBMED_18453685}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 18453685 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_18453685}}


==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Nad dependent enzyme]]
[[Category: Nad dependent enzyme]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun  4 09:53:51 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:55:37 2008''

Revision as of 15:55, 28 July 2008

File:2zea.png

Template:STRUCTURE 2zea

Crystal structure of Alcaligenes faecalis D-3-hydroxybutyrate dehydrogenase in complex with NAD+ and acetate

Template:ABSTRACT PUBMED 18453685

About this Structure

2ZEA is a Single protein structure of sequence from Alcaligenes faecalis. Full crystallographic information is available from OCA.

Reference

The structures of Alcaligenes faecalis D-3-hydroxybutyrate dehydrogenase before and after NAD+ and acetate binding suggest a dynamical reaction mechanism as a member of the SDR family., Hoque MM, Shimizu S, Hossain MT, Yamamoto T, Imamura S, Suzuki K, Tsunoda M, Amano H, Sekiguchi T, Takenaka A, Acta Crystallogr D Biol Crystallogr. 2008 May;64(Pt 5):496-505. Epub 2008, Apr 19. PMID:18453685

Page seeded by OCA on Mon Jul 28 18:55:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA