2ii5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2ii5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ii5, resolution 2.500&Aring;" /> '''Crystal structure o...)
Current revision (09:03, 21 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2ii5.jpg|left|200px]]<br /><applet load="2ii5" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="2ii5, resolution 2.500&Aring;" />
 
-
'''Crystal structure of a cubic core of the dihydrolipoamide acyltransferase (E2b) component in the branched-chain alpha-ketoacid dehydrogenase complex (BCKDC), Isobutyryl-Coenzyme A-bound form'''<br />
 
-
==Overview==
+
==Crystal structure of a cubic core of the dihydrolipoamide acyltransferase (E2b) component in the branched-chain alpha-ketoacid dehydrogenase complex (BCKDC), Isobutyryl-Coenzyme A-bound form==
-
The dihydrolipoamide acyltransferase (E2b) component of the branched-chain, alpha-ketoacid dehydrogenase complex forms a cubic scaffold that catalyzes, acyltransfer from S-acyldihydrolipoamide to CoA to produce acyl-CoA. We, have determined the first crystal structures of a mammalian (bovine) E2b, core domain with and without a bound CoA or acyl-CoA. These structures, reveal both hydrophobic and the previously unreported ionic interactions, between two-fold-related trimers that build up the cubic core. The, entrance of the dihydrolipoamide-binding site in a 30-A long active-site, channel is closed in the apo and acyl-CoA-bound structures. CoA binding to, one entrance of the channel promotes a conformational change in the, channel, resulting in the opening of the opposite dihydrolipoamide gate., Binding experiments show that the affinity of the E2b core for, dihydrolipoamide is markedly increased in the presence of CoA. The result, buttresses the model that CoA binding is responsible for the opening of, the dihydrolipoamide gate. We suggest that this gating mechanism, synchronizes the binding of the two substrates to the active-site channel, which serves as a feed-forward switch to coordinate the E2b-catalyzed, acyltransfer reaction.
+
<StructureSection load='2ii5' size='340' side='right'caption='[[2ii5]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2ii5]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2II5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2II5 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO6:ISOBUTYRYL-COENZYME+A'>CO6</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ii5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ii5 OCA], [https://pdbe.org/2ii5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ii5 RCSB], [https://www.ebi.ac.uk/pdbsum/2ii5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ii5 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ODB2_BOVIN ODB2_BOVIN] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
 +
== 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/ii/2ii5_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/main_output.php?pdb_ID=2ii5 ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
2II5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with ACT, CL and CO6 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_(2-methylpropanoyl)transferase Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.168 2.3.1.168] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2II5 OCA].
+
*[[Dihydrolipoamide dehydrogenase|Dihydrolipoamide dehydrogenase]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
A synchronized substrate-gating mechanism revealed by cubic-core structure of the bovine branched-chain alpha-ketoacid dehydrogenase complex., Kato M, Wynn RM, Chuang JL, Brautigam CA, Custorio M, Chuang DT, EMBO J. 2006 Dec 13;25(24):5983-94. Epub 2006 Nov 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17124494 17124494]
+
[[Category: Bos taurus]]
[[Category: Bos taurus]]
-
[[Category: Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Brautigam CA]]
-
[[Category: Brautigam, C.A.]]
+
[[Category: Chuang DT]]
-
[[Category: Chuang, D.T.]]
+
[[Category: Chuang JL]]
-
[[Category: Chuang, J.L.]]
+
[[Category: Custorio M]]
-
[[Category: Custorio, M.]]
+
[[Category: Kato M]]
-
[[Category: Kato, M.]]
+
[[Category: Wynn RM]]
-
[[Category: Wynn, R.M.]]
+
-
[[Category: ACT]]
+
-
[[Category: CL]]
+
-
[[Category: CO6]]
+
-
[[Category: cubic core]]
+
-
[[Category: homo trimer]]
+
-
[[Category: isobutyryl-coa-bound form]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:19:59 2007''
+

Current revision

Crystal structure of a cubic core of the dihydrolipoamide acyltransferase (E2b) component in the branched-chain alpha-ketoacid dehydrogenase complex (BCKDC), Isobutyryl-Coenzyme A-bound form

PDB ID 2ii5

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/2ii5"
Personal tools