2bp7
From Proteopedia
(New page: 200px<br /><applet load="2bp7" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bp7, resolution 2.90Å" /> '''NEW CRYSTAL FORM OF ...) |
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| - | [[Image:2bp7.gif|left|200px]]<br /><applet load="2bp7" size=" | + | [[Image:2bp7.gif|left|200px]]<br /><applet load="2bp7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bp7, resolution 2.90Å" /> | caption="2bp7, resolution 2.90Å" /> | ||
'''NEW CRYSTAL FORM OF THE PSEUDOMONAS PUTIDA BRANCHED-CHAIN DEHYDROGENASE (E1)'''<br /> | '''NEW CRYSTAL FORM OF THE PSEUDOMONAS PUTIDA BRANCHED-CHAIN DEHYDROGENASE (E1)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The pyruvate dehydrogenase (PDH) multienzyme complex is central to | + | 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== | ==About this Structure== | ||
| - | 2BP7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Active as [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] Full crystallographic information is available from [http:// | + | 2BP7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BP7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
| - | [[Category: Frank, R | + | [[Category: Frank, R A.W.]] |
| - | [[Category: Luisi, B | + | [[Category: Luisi, B F.]] |
| - | [[Category: Pei, X | + | [[Category: Pei, X Y.]] |
| - | [[Category: Perham, R | + | [[Category: Perham, R N.]] |
| - | [[Category: Pratap, J | + | [[Category: Pratap, J V.]] |
[[Category: flavoprotein]] | [[Category: flavoprotein]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: thdp cofactor]] | [[Category: thdp cofactor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:12 2008'' |
Revision as of 14:40, 21 February 2008
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NEW CRYSTAL FORM OF THE PSEUDOMONAS PUTIDA BRANCHED-CHAIN DEHYDROGENASE (E1)
Overview
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
2BP7 is a Protein complex structure of sequences from Pseudomonas putida. Active as 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring), with EC number 1.2.4.4 Full crystallographic information is available from OCA.
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:16084384
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