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.


1bxg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1bxg.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1bxg.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1bxg| PDB=1bxg | SCENE= }}
{{STRUCTURE_1bxg| PDB=1bxg | SCENE= }}
-
'''PHENYLALANINE DEHYDROGENASE STRUCTURE IN TERNARY COMPLEX WITH NAD+ AND BETA-PHENYLPROPIONATE'''
+
===PHENYLALANINE DEHYDROGENASE STRUCTURE IN TERNARY COMPLEX WITH NAD+ AND BETA-PHENYLPROPIONATE===
-
==Overview==
+
<!--
-
The molecular structures of recombinant L-phenylalanine dehydrogenase from Rhodococcus sp. M4 in two different inhibitory ternary complexes have been determined by X-ray crystallographic analyses to high resolution. Both structures show that L-phenylalanine dehydrogenase is a homodimeric enzyme with each monomer composed of distinct globular N- and C-terminal domains separated by a deep cleft containing the active site. The N-terminal domain binds the amino acid substrate and contributes to the interactions at the subunit:subunit interface. The C-terminal domain contains a typical Rossmann fold and orients the dinucleotide. The dimer has overall dimensions of approximately 82 A x 75 A x 75 A, with roughly 50 A separating the two active sites. The structures described here, namely the enzyme.NAD+.phenylpyruvate, and enzyme. NAD+.beta-phenylpropionate species, represent the first models for any amino acid dehydrogenase in a ternary complex. By analysis of the active-site interactions in these models, along with the currently available kinetic data, a detailed chemical mechanism has been proposed. This mechanism differs from those proposed to date in that it accounts for the inability of the amino acid dehydrogenases, in general, to function as hydroxy acid dehydrogenases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10029526}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10029526 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10029526}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Amino acid dehydrogenase]]
[[Category: Amino acid dehydrogenase]]
[[Category: Oxidative deamination mechanism]]
[[Category: Oxidative deamination mechanism]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:04:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:52:19 2008''

Revision as of 16:52, 30 June 2008

Image:1bxg.png

Template:STRUCTURE 1bxg

PHENYLALANINE DEHYDROGENASE STRUCTURE IN TERNARY COMPLEX WITH NAD+ AND BETA-PHENYLPROPIONATE

Template:ABSTRACT PUBMED 10029526

About this Structure

1BXG is a Protein complex structure of sequences from Rhodococcus sp.. Full crystallographic information is available from OCA.

Reference

Phenylalanine dehydrogenase from Rhodococcus sp. M4: high-resolution X-ray analyses of inhibitory ternary complexes reveal key features in the oxidative deamination mechanism., Vanhooke JL, Thoden JB, Brunhuber NM, Blanchard JS, Holden HM, Biochemistry. 1999 Feb 23;38(8):2326-39. PMID:10029526

Page seeded by OCA on Mon Jun 30 19:52:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bxg"
Personal tools