2bp7: Difference between revisions
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'''NEW CRYSTAL FORM OF THE PSEUDOMONAS PUTIDA BRANCHED-CHAIN DEHYDROGENASE (E1)''' | '''NEW CRYSTAL FORM OF THE PSEUDOMONAS PUTIDA BRANCHED-CHAIN DEHYDROGENASE (E1)''' | ||
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==Reference== | ==Reference== | ||
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] | 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: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
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[[Category: Perham, R N.]] | [[Category: Perham, R N.]] | ||
[[Category: Pratap, J V.]] | [[Category: Pratap, J V.]] | ||
[[Category: | [[Category: Flavoprotein]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
[[Category: | [[Category: Thdp cofactor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:36:15 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 20:36, 3 May 2008
NEW CRYSTAL FORM OF THE PSEUDOMONAS PUTIDA BRANCHED-CHAIN DEHYDROGENASE (E1)
OverviewOverview
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 StructureAbout this Structure
2BP7 is a Protein complex structure of sequences from Pseudomonas putida. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sat May 3 20:36:15 2008