1nr7: Difference between revisions

Revision as of 15:47, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1nr7.png

Template:STRUCTURE 1nr7

Crystal structure of apo bovine glutamate dehydrogenaseCrystal structure of apo bovine glutamate dehydrogenase

Template:ABSTRACT PUBMED 12653548

About this StructureAbout this Structure

1NR7 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation., Banerjee S, Schmidt T, Fang J, Stanley CA, Smith TJ, Biochemistry. 2003 Apr 1;42(12):3446-56. PMID:12653548

Page seeded by OCA on Mon Jul 28 15:47:16 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1nr7.gif|left|200px]]
+{{Seed}}
+[[Image:1nr7.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1nr7|  PDB=1nr7  |  SCENE=  }}
-'''Crystal structure of apo bovine glutamate dehydrogenase'''
+===Crystal structure of apo bovine glutamate dehydrogenase===
-==Overview==
+<!--
-Glutamate dehydrogenase (GDH) is found in all organisms and catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate. Unlike GDH from bacteria, mammalian GDH exhibits negative cooperativity with respect to coenzyme, activation by ADP, and inhibition by GTP. Presented here are the structures of apo bovine GDH, bovine GDH complexed with ADP, and the R463A mutant form of human GDH (huGDH) that is insensitive to ADP activation. In the absence of active site ligands, the catalytic cleft is in the open conformation, and the hexamers form long polymers in the crystal cell with more interactions than found in the abortive complex crystals. This is consistent with the fact that ADP promotes aggregation in solution. ADP is shown to bind to the second, inhibitory, NADH site yet causes activation. The beta-phosphates of the bound ADP interact with R459 (R463 in huGDH) on the pivot helix. The structure of the ADP-resistant, R463A mutant of human GDH is identical to native GDH with the exception of the truncated side chain on the pivot helix. Together, these results strongly suggest that ADP activates by facilitating the opening of the catalytic cleft. From alignment of GDH from various sources, it is likely that the antenna evolved in the protista prior to the formation of purine regulatory sites. This suggests that there was some selective advantage of the antenna itself and that animals evolved new functions for GDH through the addition of allosteric regulation.
+The line below this paragraph, {{ABSTRACT_PUBMED_12653548}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12653548 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12653548}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Stanley, C A.]]
 [[Category: Apo bovine glutamate dehydrogenase regulation allostery]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:53:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:47:16 2008''