1a4s: Difference between revisions
New page: left|200px<br /><applet load="1a4s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a4s, resolution 2.10Å" /> '''BETAINE ALDEHYDE DEH... |
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[[Image:1a4s.gif|left|200px]]<br /><applet load="1a4s" size=" | [[Image:1a4s.gif|left|200px]]<br /><applet load="1a4s" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1a4s, resolution 2.10Å" /> | caption="1a4s, resolution 2.10Å" /> | ||
'''BETAINE ALDEHYDE DEHYDROGENASE FROM COD LIVER'''<br /> | '''BETAINE ALDEHYDE DEHYDROGENASE FROM COD LIVER'''<br /> | ||
==Overview== | ==Overview== | ||
The three-dimensional structure of betaine aldehyde dehydrogenase, the | 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== | ==About this Structure== | ||
1A4S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gadus_callarias Gadus callarias]. Active as [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] Full crystallographic information is available from [http:// | 1A4S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gadus_callarias Gadus callarias]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4S OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Gadus callarias]] | [[Category: Gadus callarias]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ahmad, M | [[Category: Ahmad, M El.]] | ||
[[Category: Eklund, H.]] | [[Category: Eklund, H.]] | ||
[[Category: Hjelmqvist, L.]] | [[Category: Hjelmqvist, L.]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:51 2008'' | ||
Revision as of 12:40, 21 February 2008
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BETAINE ALDEHYDE DEHYDROGENASE FROM COD LIVER
OverviewOverview
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 StructureAbout this Structure
1A4S is a Single protein structure of sequence from Gadus callarias. Active as Betaine-aldehyde dehydrogenase, with EC number 1.2.1.8 Full crystallographic information is available from OCA.
ReferenceReference
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
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