We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1nm8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1nm8" [edit=sysop:move=sysop])
Line 1: Line 1:
-
[[Image:1nm8.png|left|200px]]
+
==Structure of Human Carnitine Acetyltransferase: Molecular Basis for Fatty Acyl Transfer==
 +
<StructureSection load='1nm8' size='340' side='right' caption='[[1nm8]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1nm8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NM8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NM8 FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRAT OR CAT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
 +
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
 +
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nm8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nm8 RCSB], [http://www.ebi.ac.uk/pdbsum/1nm8 PDBsum]</span></td></tr>
 +
<table>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nm/1nm8_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
{{STRUCTURE_1nm8| PDB=1nm8 | SCENE= }}
+
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<ref>PMID:12562770</ref>
-
===Structure of Human Carnitine Acetyltransferase: Molecular Basis for Fatty Acyl Transfer===
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
-
{{ABSTRACT_PUBMED_12562770}}
+
==See Also==
-
 
+
*[[Carnitine acetyltransferase|Carnitine acetyltransferase]]
-
==About this Structure==
+
== References ==
-
[[1nm8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NM8 OCA].
+
<references/>
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
<ref group="xtra">PMID:012562770</ref><references group="xtra"/>
+
[[Category: Carnitine O-acetyltransferase]]
[[Category: Carnitine O-acetyltransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]

Revision as of 16:27, 28 September 2014

Structure of Human Carnitine Acetyltransferase: Molecular Basis for Fatty Acyl Transfer

1nm8, resolution 1.60Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nm8"
Views
Personal tools
Navigation
Toolbox