This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2bp7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2bp7.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2bp7.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2bp7| PDB=2bp7 | SCENE= }}
{{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)===
-
==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 line below this paragraph, {{ABSTRACT_PUBMED_16084384}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16084384 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16084384}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Thdp cofactor]]
[[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 Tue Jul 29 14:39:27 2008''

Revision as of 11:39, 29 July 2008

Image:2bp7.png

Template:STRUCTURE 2bp7

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

Template:ABSTRACT PUBMED 16084384

About this Structure

2BP7 is a Protein complex structure of sequences from Pseudomonas putida. 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

Page seeded by OCA on Tue Jul 29 14:39:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bp7"
Personal tools