1a4s

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[[Image:1a4s.gif|left|200px]]
[[Image:1a4s.gif|left|200px]]
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{{Structure
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|PDB= 1a4s |SIZE=350|CAPTION= <scene name='initialview01'>1a4s</scene>, resolution 2.10&Aring;
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The line below this paragraph, containing "STRUCTURE_1a4s", creates the "Structure Box" on the page.
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|SITE=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Betaine-aldehyde_dehydrogenase Betaine-aldehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.8 1.2.1.8] </span>
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{{STRUCTURE_1a4s| PDB=1a4s | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4s OCA], [http://www.ebi.ac.uk/pdbsum/1a4s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a4s RCSB]</span>
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'''BETAINE ALDEHYDE DEHYDROGENASE FROM COD LIVER'''
'''BETAINE ALDEHYDE DEHYDROGENASE FROM COD LIVER'''
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[[Category: Jornvall, H.]]
[[Category: Jornvall, H.]]
[[Category: Ramaswamy, S.]]
[[Category: Ramaswamy, S.]]
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[[Category: aldehyde oxidation]]
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[[Category: Aldehyde oxidation]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:48:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:33:12 2008''
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Revision as of 06:48, 2 May 2008

Template:STRUCTURE 1a4s

BETAINE ALDEHYDE DEHYDROGENASE FROM COD LIVER


Overview

The three-dimensional structure of betaine aldehyde dehydrogenase, the most abundant aldehyde dehydrogenase (ALDH) of cod liver, has been determined at 2.1 A resolution by the X-ray crystallographic method of molecular replacement. This enzyme represents a novel structure of the highly multiple ALDH, with at least 12 distinct classes in humans. This betaine ALDH of class 9 is different from the two recently determined ALDH structures (classes 2 and 3). Like these, the betaine ALDH structure has three domains, one coenzyme binding domain, one catalytic domain, and one oligomerization domain. Crystals grown in the presence or absence of NAD+ have very similar structures and no significant conformational change occurs upon coenzyme binding. This is probably due to the tight interactions between domains within the subunit and between subunits in the tetramer. The oligomerization domains link the catalytic domains together into two 20-stranded pleated sheet structures. The overall structure is similar to that of the tetrameric bovine class 2 and dimeric rat class 3 ALDH, but the coenzyme binding with the nicotinamide in anti conformation, resembles that of class 2 rather than of class 3.

About this Structure

1A4S is a Single protein structure of sequence from Gadus callarias. Full crystallographic information is available from OCA.

Reference

Structure of betaine aldehyde dehydrogenase at 2.1 A resolution., Johansson K, El-Ahmad M, Ramaswamy S, Hjelmqvist L, Jornvall H, Eklund H, Protein Sci. 1998 Oct;7(10):2106-17. PMID:9792097 Page seeded by OCA on Fri May 2 09:48:32 2008

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