1nm8
From Proteopedia
(New page: 200px<br /> <applet load="1nm8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nm8, resolution 1.6Å" /> '''Structure of Human C...) |
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| - | [[Image:1nm8.gif|left|200px]]<br /> | + | [[Image:1nm8.gif|left|200px]]<br /><applet load="1nm8" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1nm8, resolution 1.6Å" /> | caption="1nm8, resolution 1.6Å" /> | ||
'''Structure of Human Carnitine Acetyltransferase: Molecular Basis for Fatty Acyl Transfer'''<br /> | '''Structure of Human Carnitine Acetyltransferase: Molecular Basis for Fatty Acyl Transfer'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Carnitine acyltransferases are a family of ubiquitous enzymes that play a | + | Carnitine acyltransferases are a family of ubiquitous enzymes that play a pivotal role in cellular energy metabolism. We report here the x-ray structure of human carnitine acetyltransferase to a 1.6-A resolution. This structure reveals a monomeric protein of two equally sized alpha/beta domains. Each domain is shown to have a partially similar fold to other known but oligomeric enzymes that are also involved in group-transfer reactions. The unique monomeric arrangement of the two domains constitutes a central narrow active site tunnel, indicating a likely universal feature for all members of the carnitine acyltransferase family. Superimposition of the substrate complex of a related protein, dihydrolipoyl trans-acetylase, reveals that both substrates localize to the active site tunnel of human carnitine acetyltransferase, suggesting the location of the ligand binding sites for carnitine and coenzyme A. Most significantly, this structure provides critical insights into the molecular basis for fatty acyl chain transfer and a possible common mechanism among a wide range of acyltransferases utilizing a catalytic dyad. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NM8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Carnitine_O-acetyltransferase Carnitine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.7 2.3.1.7] Full crystallographic information is available from [http:// | + | 1NM8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Carnitine_O-acetyltransferase Carnitine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.7 2.3.1.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NM8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: two equally sized domains]] | [[Category: two equally sized domains]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:34 2008'' |
Revision as of 12:07, 21 February 2008
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Structure of Human Carnitine Acetyltransferase: Molecular Basis for Fatty Acyl Transfer
Contents |
Overview
Carnitine acyltransferases are a family of ubiquitous enzymes that play a pivotal role in cellular energy metabolism. We report here the x-ray structure of human carnitine acetyltransferase to a 1.6-A resolution. This structure reveals a monomeric protein of two equally sized alpha/beta domains. Each domain is shown to have a partially similar fold to other known but oligomeric enzymes that are also involved in group-transfer reactions. The unique monomeric arrangement of the two domains constitutes a central narrow active site tunnel, indicating a likely universal feature for all members of the carnitine acyltransferase family. Superimposition of the substrate complex of a related protein, dihydrolipoyl trans-acetylase, reveals that both substrates localize to the active site tunnel of human carnitine acetyltransferase, suggesting the location of the ligand binding sites for carnitine and coenzyme A. Most significantly, this structure provides critical insights into the molecular basis for fatty acyl chain transfer and a possible common mechanism among a wide range of acyltransferases utilizing a catalytic dyad.
Disease
Known disease associated with this structure: Carnitine acetyltransferase deficiency (1) OMIM:[600184]
About this Structure
1NM8 is a Single protein structure of sequence from Homo sapiens. Active as Carnitine O-acetyltransferase, with EC number 2.3.1.7 Full crystallographic information is available from OCA.
Reference
Structure of human carnitine acetyltransferase. Molecular basis for fatty acyl transfer., Wu D, Govindasamy L, Lian W, Gu Y, Kukar T, Agbandje-McKenna M, McKenna R, J Biol Chem. 2003 Apr 11;278(15):13159-65. Epub 2003 Jan 31. PMID:12562770
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