2bp7: Difference between revisions

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[[Image:2bp7.gif|left|200px]]<br /><applet load="2bp7" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2bp7.gif|left|200px]]<br /><applet load="2bp7" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2bp7, resolution 2.90Å" />

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

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2BP7 OCA].

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==

Line 14:

[[Category: Protein complex]]

[[Category: Pseudomonas putida]]

[[Category: Frank, R.A.W.]]

[[Category: Frank, R A.W.]]

[[Category: Luisi, B.F.]]

[[Category: Luisi, B F.]]

[[Category: Pei, X.Y.]]

[[Category: Pei, X Y.]]

[[Category: Perham, R.N.]]

[[Category: Perham, R N.]]

[[Category: Pratap, J.V.]]

[[Category: Pratap, J V.]]

[[Category: flavoprotein]]

[[Category: oxidoreductase]]

[[Category: thdp cofactor]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 08:51:~~50 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:12 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2bp7.gif|left|200px]]<br /><applet load="2bp7" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2bp7.gif|left|200px]]<br /><applet load="2bp7" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2bp7, resolution 2.90&Aring;" />
 '''NEW CRYSTAL FORM OF THE PSEUDOMONAS PUTIDA BRANCHED-CHAIN DEHYDROGENASE (E1)'''<br />
 ==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.
+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==
-BP7 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BP7 OCA].
+BP7 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==
@@ Line 14: / Line 14: @@
 [[Category: Protein complex]]
 [[Category: Pseudomonas putida]]
-[[Category: Frank, R.A.W.]]
+[[Category: Frank, R A.W.]]
-[[Category: Luisi, B.F.]]
+[[Category: Luisi, B F.]]
-[[Category: Pei, X.Y.]]
+[[Category: Pei, X Y.]]
-[[Category: Perham, R.N.]]
+[[Category: Perham, R N.]]
-[[Category: Pratap, J.V.]]
+[[Category: Pratap, J V.]]
 [[Category: flavoprotein]]
 [[Category: oxidoreductase]]
 [[Category: thdp cofactor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:51:50 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:12 2008''