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[[Image:2bp7.gif|left|200px]]
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{{STRUCTURE_2bp7|  PDB=2bp7  |  SCENE=  }}
'''NEW CRYSTAL FORM OF THE PSEUDOMONAS PUTIDA BRANCHED-CHAIN DEHYDROGENASE (E1)'''


==New crystal form of the Pseudomonas putida branched-chain dehydrogenase (E1)==
<StructureSection load='2bp7' size='340' side='right'caption='[[2bp7]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bp7]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BP7 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]] 2.9&#8491;</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=2bp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bp7 OCA], [https://pdbe.org/2bp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bp7 RCSB], [https://www.ebi.ac.uk/pdbsum/2bp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bp7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ODBA_PSEPU ODBA_PSEPU] 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/bp/2bp7_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=2bp7 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The pyruvate dehydrogenase (PDH) multienzyme complex is central to oxidative metabolism. We present the first crystal structure of a complex between pyruvate decarboxylase (E1) and the peripheral subunit binding domain (PSBD) of the dihydrolipoyl acetyltransferase (E2). The interface is dominated by a "charge zipper" of networked salt bridges. Remarkably, the PSBD uses essentially the same zipper to alternately recognize the dihydrolipoyl dehydrogenase (E3) component of the PDH assembly. The PSBD achieves this dual recognition largely through the addition of a network of interfacial water molecules unique to the E1-PSBD complex. These structural comparisons illuminate our observations that the formation of this water-rich E1-E2 interface is largely enthalpy driven, whereas that of the E3-PSBD complex (from which water is excluded) is entropy driven. Interfacial water molecules thus diversify surface complementarity and contribute to avidity, enthalpically. Additionally, the E1-PSBD structure provides insight into the organization and active site coupling within the approximately 9 MDa PDH complex.


==Overview==
The molecular origins of specificity in the assembly of a multienzyme complex.,Frank RA, Pratap JV, Pei XY, Perham RN, Luisi BF Structure. 2005 Aug;13(8):1119-30. PMID:16084384<ref>PMID:16084384</ref>
The pyruvate dehydrogenase (PDH) multienzyme complex is central to oxidative metabolism. We present the first crystal structure of a complex between pyruvate decarboxylase (E1) and the peripheral subunit binding domain (PSBD) of the dihydrolipoyl acetyltransferase (E2). The interface is dominated by a "charge zipper" of networked salt bridges. Remarkably, the PSBD uses essentially the same zipper to alternately recognize the dihydrolipoyl dehydrogenase (E3) component of the PDH assembly. The PSBD achieves this dual recognition largely through the addition of a network of interfacial water molecules unique to the E1-PSBD complex. These structural comparisons illuminate our observations that the formation of this water-rich E1-E2 interface is largely enthalpy driven, whereas that of the E3-PSBD complex (from which water is excluded) is entropy driven. Interfacial water molecules thus diversify surface complementarity and contribute to avidity, enthalpically. Additionally, the E1-PSBD structure provides insight into the organization and active site coupling within the approximately 9 MDa PDH complex.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2BP7 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BP7 OCA].
</div>
<div class="pdbe-citations 2bp7" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The molecular origins of specificity in the assembly of a multienzyme complex., Frank RA, Pratap JV, Pei XY, Perham RN, Luisi BF, Structure. 2005 Aug;13(8):1119-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16084384 16084384]
*[[2-oxoisovalerate dehydrogenase 3D structures|2-oxoisovalerate dehydrogenase 3D structures]]
[[Category: Protein complex]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Frank, R A.W.]]
[[Category: Frank RAW]]
[[Category: Luisi, B F.]]
[[Category: Luisi BF]]
[[Category: Pei, X Y.]]
[[Category: Pei XY]]
[[Category: Perham, R N.]]
[[Category: Perham RN]]
[[Category: Pratap, J V.]]
[[Category: Pratap JV]]
[[Category: Flavoprotein]]
[[Category: Oxidoreductase]]
[[Category: Thdp cofactor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:36:15 2008''