3eq6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "3eq6" [edit=sysop:move=sysop])
Line 1: Line 1:
-
[[Image:3eq6.png|left|200px]]
+
==Crystal structure of human acyl-CoA synthetase medium-chain family member 2A (L64P mutation) in a ternary complex with products==
 +
<StructureSection load='3eq6' size='340' side='right' caption='[[3eq6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3eq6]] is a 2 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=3EQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EQ6 FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=BCO:S-[2-[3-[[(2S)-4-[[[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-4-HYDROXY-3-PHOSPHONOOXY-OXOLAN-2-YL]METHOXY-HYDROXY-PHOSPHORYL]OXY-HYDROXY-PHOSPHORYL]OXY-2-HYDROXY-3,3-DIMETHYL-BUTANOYL]AMINO]PROPANOYLAMINO]ETHYL]+BUTANETHIOATE'>BCO</scene></td></tr>
 +
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3c5e|3c5e]], [[3day|3day]], [[3b7w|3b7w]]</td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACSM2A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
 +
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Butyrate--CoA_ligase Butyrate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.2 6.2.1.2] </span></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3eq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eq6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3eq6 RCSB], [http://www.ebi.ac.uk/pdbsum/3eq6 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/eq/3eq6_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 ==
 +
Acyl-CoA synthetases belong to the superfamily of adenylate-forming enzymes, and catalyze the two-step activation of fatty acids or carboxylate-containing xenobiotics. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Here, we report the first crystal structure of a medium-chain acyl-CoA synthetase ACSM2A, in a series of substrate/product/cofactor complexes central to the catalytic mechanism. We observed a substantial rearrangement between the N- and C-terminal domains, driven purely by the identity of the bound ligand in the active site. Our structures allowed us to identify the presence or absence of the ATP pyrophosphates as the conformational switch, and elucidated new mechanistic details, including the role of invariant Lys557 and a divalent magnesium ion in coordinating the ATP pyrophosphates, as well as the involvement of a Gly-rich P-loop and the conserved Arg472-Glu365 salt bridge in the domain rearrangement.
-
<!--
+
Structural snapshots for the conformation-dependent catalysis by human medium-chain acyl-coenzyme A synthetase ACSM2A.,Kochan G, Pilka ES, von Delft F, Oppermann U, Yue WW J Mol Biol. 2009 May 22;388(5):997-1008. Epub 2009 Apr 1. PMID:19345228<ref>PMID:19345228</ref>
-
The line below this paragraph, containing "STRUCTURE_3eq6", creates the "Structure Box" on the page.
+
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
-
or leave the SCENE parameter empty for the default display.
+
-
-->
+
-
{{STRUCTURE_3eq6| PDB=3eq6 | SCENE= }}
+
-
===Crystal structure of human acyl-CoA synthetase medium-chain family member 2A (L64P mutation) in a ternary complex with products===
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
 
+
== References ==
-
<!--
+
<references/>
-
The line below this paragraph, {{ABSTRACT_PUBMED_19345228}}, adds the Publication Abstract to the page
+
__TOC__
-
(as it appears on PubMed at http://www.pubmed.gov), where 19345228 is the PubMed ID number.
+
</StructureSection>
-
-->
+
-
{{ABSTRACT_PUBMED_19345228}}
+
-
 
+
-
==About this Structure==
+
-
[[3eq6]] is a 2 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=3EQ6 OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:19345228</ref><references group="xtra"/>
+
[[Category: Butyrate--CoA ligase]]
[[Category: Butyrate--CoA ligase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Arrowsmith, C H.]]
+
[[Category: Arrowsmith, C H]]
-
[[Category: Bhatia, C.]]
+
[[Category: Bhatia, C]]
-
[[Category: Bountra, C.]]
+
[[Category: Bountra, C]]
-
[[Category: Edwards, A M.]]
+
[[Category: Edwards, A M]]
-
[[Category: Kochan, G.]]
+
[[Category: Kochan, G]]
-
[[Category: Oppermann, U.]]
+
[[Category: Oppermann, U]]
-
[[Category: Pilka, E S.]]
+
[[Category: Pilka, E S]]
-
[[Category: SGC, Structural Genomics Consortium.]]
+
[[Category: Structural genomic]]
-
[[Category: Weigelt, J.]]
+
[[Category: Weigelt, J]]
-
[[Category: Yue, W W.]]
+
[[Category: Yue, W W]]
-
[[Category: Delft, F Von.]]
+
[[Category: Delft, F Von]]
 +
[[Category: Atp-binding]]
 +
[[Category: Fatty acid metabolism]]
 +
[[Category: Ligase]]
 +
[[Category: Lipid metabolism]]
 +
[[Category: Magnesium]]
 +
[[Category: Metal-binding]]
 +
[[Category: Middle-chain acyl-coa synthetase]]
 +
[[Category: Mitochondrion]]
 +
[[Category: Nucleotide-binding polymorphism]]
 +
[[Category: Sgc]]
 +
[[Category: Transit peptide]]
 +
[[Category: Xenobiotic/medium-chain fatty acid-coa ligase]]

Revision as of 08:53, 26 November 2014

Crystal structure of human acyl-CoA synthetase medium-chain family member 2A (L64P mutation) in a ternary complex with products

3eq6, resolution 2.40Å

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/3eq6"
Personal tools