2ii5: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(10 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:2ii5.png|left|200px]]


<!--
==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 line below this paragraph, containing "STRUCTURE_2ii5", creates the "Structure Box" on the page.
<StructureSection load='2ii5' size='340' side='right'caption='[[2ii5]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_2ii5| PDB=2ii5 |  SCENE= }}
<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>


===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===
==See Also==
 
*[[Dihydrolipoamide dehydrogenase|Dihydrolipoamide dehydrogenase]]
 
__TOC__
<!--
</StructureSection>
The line below this paragraph, {{ABSTRACT_PUBMED_17124494}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17124494 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17124494}}
 
==About this Structure==
2II5 is a [[Single protein]] structure of sequence from [http://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].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/17124494 17124494]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Brautigam, C A.]]
[[Category: Brautigam CA]]
[[Category: Chuang, D T.]]
[[Category: Chuang DT]]
[[Category: Chuang, J L.]]
[[Category: Chuang JL]]
[[Category: Custorio, M.]]
[[Category: Custorio M]]
[[Category: Kato, M.]]
[[Category: Kato M]]
[[Category: Wynn, R M.]]
[[Category: Wynn RM]]
[[Category: Cubic core]]
[[Category: Homo trimer]]
[[Category: Isobutyryl-coa-bound form]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:15:18 2008''

Latest revision as of 12:03, 21 February 2024

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 formCrystal 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

Structural highlights

2ii5 is a 8 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2ii5, resolution 2.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2ii5&oldid=4062014"