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[[Image:2bp7.gif|left|200px]]


{{Structure
==New crystal form of the Pseudomonas putida branched-chain dehydrogenase (E1)==
|PDB= 2bp7 |SIZE=350|CAPTION= <scene name='initialview01'>2bp7</scene>, resolution 2.90&Aring;
<StructureSection load='2bp7' size='340' side='right'caption='[[2bp7]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<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>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_dehydrogenase_(2-methylpropanoyl-transferring) 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.4 1.2.4.4] </span>
</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>
|GENE=  
<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>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bp7 OCA], [http://www.ebi.ac.uk/pdbsum/2bp7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bp7 RCSB]</span>
[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.


'''NEW CRYSTAL FORM OF THE PSEUDOMONAS PUTIDA BRANCHED-CHAIN DEHYDROGENASE (E1)'''
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2bp7" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[2-oxoisovalerate dehydrogenase 3D structures|2-oxoisovalerate dehydrogenase 3D structures]]
 
== References ==
==About this Structure==
<references/>
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].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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]
[[Category: 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]]
[[Category: Protein complex]]
[[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 Mon Mar 31 02:09:40 2008''

Latest revision as of 16:51, 13 December 2023

New crystal form of the Pseudomonas putida branched-chain dehydrogenase (E1)New crystal form of the Pseudomonas putida branched-chain dehydrogenase (E1)

Structural highlights

2bp7 is a 8 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

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

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Frank RA, Pratap JV, Pei XY, Perham RN, Luisi BF. The molecular origins of specificity in the assembly of a multienzyme complex. Structure. 2005 Aug;13(8):1119-30. PMID:16084384 doi:10.1016/j.str.2005.04.021

2bp7, resolution 2.90Å

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