1zcj: Difference between revisions
New page: left|200px<br /><applet load="1zcj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zcj, resolution 1.90Å" /> '''Crystal structure of... |
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[[Image:1zcj.gif|left|200px]]<br /><applet load="1zcj" size=" | [[Image:1zcj.gif|left|200px]]<br /><applet load="1zcj" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1zcj, resolution 1.90Å" /> | caption="1zcj, resolution 1.90Å" /> | ||
'''Crystal structure of 3-hydroxyacyl-CoA dehydrogenase'''<br /> | '''Crystal structure of 3-hydroxyacyl-CoA dehydrogenase'''<br /> | ||
==Overview== | ==Overview== | ||
The 1.9 A structure of the C-terminal dehydrogenase part of the rat | The 1.9 A structure of the C-terminal dehydrogenase part of the rat peroxisomal monomeric multifunctional enzyme type 1 (MFE-1) has been determined. In this construct (residues 260-722 and referred to as MFE1-DH) the N-terminal hydratase part of MFE-1 has been deleted. The structure of MFE1-DH shows that it consists of an N-terminal helix, followed by a Rossmann-fold domain (domain C), followed by two tightly associated helical domains (domains D and E), which have similar topology. The structure of MFE1-DH is compared with the two known homologous structures: human mitochondrial 3-hydroxyacyl-CoA dehydrogenase (HAD; sequence identity is 33%) (which is dimeric and monofunctional) and with the dimeric multifunctional alpha-chain (alphaFOM; sequence identity is 28%) of the bacterial fatty acid beta-oxidation alpha2beta2-multienzyme complex. Like MFE-1, alphaFOM has an N-terminal hydratase part and a C-terminal dehydrogenase part, and the structure comparisons show that the N-terminal helix of MFE1-DH corresponds to the alphaFOM linker helix, located between its hydratase and dehydrogenase part. It is also shown that this helix corresponds to the C-terminal helix-10 of the hydratase/isomerase superfamily, suggesting that functionally it belongs to the N-terminal hydratase part of MFE-1. | ||
==About this Structure== | ==About this Structure== | ||
1ZCJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/3-hydroxyacyl-CoA_dehydrogenase 3-hydroxyacyl-CoA dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.35 1.1.1.35] Full crystallographic information is available from [http:// | 1ZCJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/3-hydroxyacyl-CoA_dehydrogenase 3-hydroxyacyl-CoA dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.35 1.1.1.35] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZCJ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hiltunen, J | [[Category: Hiltunen, J K.]] | ||
[[Category: Kiema, T | [[Category: Kiema, T R.]] | ||
[[Category: Taskinen, J | [[Category: Taskinen, J P.]] | ||
[[Category: Wierenga, R | [[Category: Wierenga, R K.]] | ||
[[Category: fatty acid beta oxidation]] | [[Category: fatty acid beta oxidation]] | ||
[[Category: l-bifunctional enzyme]] | [[Category: l-bifunctional enzyme]] | ||
| Line 25: | Line 25: | ||
[[Category: rat]] | [[Category: rat]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:13 2008'' | ||
Revision as of 14:14, 21 February 2008
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Crystal structure of 3-hydroxyacyl-CoA dehydrogenase
Overview
The 1.9 A structure of the C-terminal dehydrogenase part of the rat peroxisomal monomeric multifunctional enzyme type 1 (MFE-1) has been determined. In this construct (residues 260-722 and referred to as MFE1-DH) the N-terminal hydratase part of MFE-1 has been deleted. The structure of MFE1-DH shows that it consists of an N-terminal helix, followed by a Rossmann-fold domain (domain C), followed by two tightly associated helical domains (domains D and E), which have similar topology. The structure of MFE1-DH is compared with the two known homologous structures: human mitochondrial 3-hydroxyacyl-CoA dehydrogenase (HAD; sequence identity is 33%) (which is dimeric and monofunctional) and with the dimeric multifunctional alpha-chain (alphaFOM; sequence identity is 28%) of the bacterial fatty acid beta-oxidation alpha2beta2-multienzyme complex. Like MFE-1, alphaFOM has an N-terminal hydratase part and a C-terminal dehydrogenase part, and the structure comparisons show that the N-terminal helix of MFE1-DH corresponds to the alphaFOM linker helix, located between its hydratase and dehydrogenase part. It is also shown that this helix corresponds to the C-terminal helix-10 of the hydratase/isomerase superfamily, suggesting that functionally it belongs to the N-terminal hydratase part of MFE-1.
About this Structure
1ZCJ is a Single protein structure of sequence from Rattus norvegicus. Active as 3-hydroxyacyl-CoA dehydrogenase, with EC number 1.1.1.35 Full crystallographic information is available from OCA.
Reference
Structural studies of MFE-1: the 1.9 A crystal structure of the dehydrogenase part of rat peroxisomal MFE-1., Taskinen JP, Kiema TR, Hiltunen JK, Wierenga RK, J Mol Biol. 2006 Jan 27;355(4):734-46. Epub 2005 Nov 18. PMID:16330050
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