1hrd: Difference between revisions

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New page: left|200px<br /><applet load="1hrd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hrd, resolution 1.96Å" /> '''GLUTAMATE DEHYDROGEN...
 
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[[Image:1hrd.gif|left|200px]]<br /><applet load="1hrd" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hrd, resolution 1.96&Aring;" />
'''GLUTAMATE DEHYDROGENASE'''<br />


==Overview==
==GLUTAMATE DEHYDROGENASE==
BACKGROUND: The hyperthermophile Pyrococcus furiosus is one of the most, thermostable organisms known, with an optimum growth temperature of 100, degrees C. The proteins from this organism display extreme, thermostability. We have undertaken the structure determination of, glutamate dehydrogenase from P. furiosus in order to gain further insights, into the relationship between molecular structure and thermal stability., RESULTS: The structure of P. furiosus glutamate dehydrogenase, a, homohexameric enzyme, has been determined at 2.2 A resolution and compared, with the structure of glutamate dehydrogenase from the mesophile, Clostridium symbiosum. CONCLUSIONS: Comparison of the structures of these, two enzymes has revealed one major difference: the structure of the, hyperthermophilic enzyme contains a striking series of ion-pair networks, on the surface of the protein subunits and buried at both interdomain and, intersubunit interfaces. We propose that the formation of such extended, networks may represent a major stabilizing feature associated with the, adaptation of enzymes to extreme temperatures.
<StructureSection load='1hrd' size='340' side='right'caption='[[1hrd]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hrd]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_symbiosum Clostridium symbiosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HRD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.96&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hrd OCA], [https://pdbe.org/1hrd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hrd RCSB], [https://www.ebi.ac.uk/pdbsum/1hrd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hrd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DHE2_CLOSY DHE2_CLOSY]
== 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/hr/1hrd_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=1hrd ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1HRD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_symbiosum Clostridium symbiosum]. Active as [http://en.wikipedia.org/wiki/Glutamate_dehydrogenase Glutamate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.2 1.4.1.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HRD OCA].
*[[Glutamate dehydrogenase 3D structures|Glutamate dehydrogenase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures., Yip KS, Stillman TJ, Britton KL, Artymiuk PJ, Baker PJ, Sedelnikova SE, Engel PC, Pasquo A, Chiaraluce R, Consalvi V, Structure. 1995 Nov 15;3(11):1147-58. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8591026 8591026]
[[Category: Large Structures]]
[[Category: Clostridium symbiosum]]
[[Category: Baker PJ]]
[[Category: Glutamate dehydrogenase]]
[[Category: Britton KL]]
[[Category: Single protein]]
[[Category: Rice DW]]
[[Category: Baker, P.J.]]
[[Category: Stillman TJ]]
[[Category: Britton, K.L.]]
[[Category: Rice, D.W.]]
[[Category: Stillman, T.J.]]
[[Category: nad]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:46:50 2007''

Latest revision as of 10:29, 7 February 2024

GLUTAMATE DEHYDROGENASEGLUTAMATE DEHYDROGENASE

Structural highlights

1hrd is a 3 chain structure with sequence from Clostridium symbiosum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.96Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DHE2_CLOSY

Evolutionary Conservation

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

See Also

1hrd, resolution 1.96Å

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