1nr7: Difference between revisions

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[[Image:1nr7.gif|left|200px]]


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==Crystal structure of apo bovine glutamate dehydrogenase==
The line below this paragraph, containing "STRUCTURE_1nr7", creates the "Structure Box" on the page.
<StructureSection load='1nr7' size='340' side='right'caption='[[1nr7]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1nr7]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NR7 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nr7 OCA], [https://pdbe.org/1nr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nr7 RCSB], [https://www.ebi.ac.uk/pdbsum/1nr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nr7 ProSAT]</span></td></tr>
{{STRUCTURE_1nr7| PDB=1nr7 |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/DHE3_BOVIN DHE3_BOVIN] May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).<ref>PMID:14659072</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nr/1nr7_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nr7 ConSurf].
<div style="clear:both"></div>


'''Crystal structure of apo bovine glutamate dehydrogenase'''
==See Also==
 
*[[Glutamate dehydrogenase 3D structures|Glutamate dehydrogenase 3D structures]]
 
== References ==
==Overview==
<references/>
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.
__TOC__
 
</StructureSection>
==About this Structure==
1NR7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NR7 OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/12653548 12653548]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Banerjee, S.]]
[[Category: Banerjee S]]
[[Category: Fang, J.]]
[[Category: Fang J]]
[[Category: Schmidt, T.]]
[[Category: Schmidt T]]
[[Category: Smith, T J.]]
[[Category: Smith TJ]]
[[Category: Stanley, C A.]]
[[Category: Stanley CA]]
[[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''

Latest revision as of 10:59, 14 February 2024

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

Structural highlights

1nr7 is a 12 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DHE3_BOVIN May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Kim DW, Eum WS, Jang SH, Yoon CS, Kim YH, Choi SH, Choi HS, Kim SY, Kwon HY, Kang JH, Kwon OS, Cho SW, Park J, Choi SY. Molecular gene cloning, expression, and characterization of bovine brain glutamate dehydrogenase. J Biochem Mol Biol. 2003 Nov 30;36(6):545-51. PMID:14659072 doi:<ARTICLE_ID IdType=doi> <ARTICLE_ID IdType=doi>

1nr7, resolution 3.30Å

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