1v9l

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{{Seed}}
 
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[[Image:1v9l.png|left|200px]]
 
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==L-glutamate dehydrogenase from Pyrobaculum islandicum complexed with NAD==
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The line below this paragraph, containing "STRUCTURE_1v9l", creates the "Structure Box" on the page.
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<StructureSection load='1v9l' size='340' side='right'caption='[[1v9l]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1v9l]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_islandicum Pyrobaculum islandicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V9L FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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{{STRUCTURE_1v9l| PDB=1v9l | SCENE= }}
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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=1v9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v9l OCA], [https://pdbe.org/1v9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v9l RCSB], [https://www.ebi.ac.uk/pdbsum/1v9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v9l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9Y8I4_PYRIS Q9Y8I4_PYRIS]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v9/1v9l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1v9l ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The extremely thermostable NAD-dependent glutamate dehydrogenase (NAD-GluDH) from Pyrobaculum islandicum, a member of the Crenarchaeota, was crystallized, and its 3D structure has been determined by X-ray diffraction methods. The homohexameric structure of Pb. islandicum glutamate dehydrogenase (Pis-GluDH) was solved and refined at a resolution of 2.9A with a crystallographic R-factor of 19.9% (Rfree 26.0%). The structure indicates that each subunit consists of two domains separated by a deep cleft containing an active site. The secondary structural elements and catalytically important residues of the enzyme were highly conserved among the NAD(P)-dependent GluDHs from other sources. A structural comparison of Pis-GluDH with other NAD(P)-dependent GluDHs suggests that a significant difference in the alpha8-loop-alpha9 region of this enzyme is associated with its coenzyme specificity. From the analysis of the 3D structure, hydrophobic interactions between intersubunits were found to be important features for the enzyme oligomerization. It has been reported that Pis-GluDH is highly thermostable, like the GluDH of the hyperthermophilic archaeum Pyrococcus furiosus, and the increase in the intersubunit ion pair networks is responsible for the extreme thermostability of the Pc. furiosus enzyme. However, the number of intersubunit ion pairs in the Pis-GluDH molecules is much smaller than those of the Pc. furiosus GluDH. The number of hydrophobic interactions at the intersubunit interfaces were increased and responsible for the extremely high thermostability. This indicates that the major molecular strategy for high thermostability of the GluDHs may be different for each hyperthermophile.
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===L-glutamate dehydrogenase from Pyrobaculum islandicum complexed with NAD===
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The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum.,Bhuiya MW, Sakuraba H, Ohshima T, Imagawa T, Katunuma N, Tsuge H J Mol Biol. 2005 Jan 14;345(2):325-37. PMID:15571725<ref>PMID:15571725</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1v9l" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15571725}}, adds the Publication Abstract to the page
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*[[Glutamate dehydrogenase 3D structures|Glutamate dehydrogenase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15571725 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15571725}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1V9L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_islandicum Pyrobaculum islandicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9L OCA].
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==Reference==
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The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum., Bhuiya MW, Sakuraba H, Ohshima T, Imagawa T, Katunuma N, Tsuge H, J Mol Biol. 2005 Jan 14;345(2):325-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15571725 15571725]
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Enzymological characteristics of the hyperthermostable NAD-dependent glutamate dehydrogenase from the archaeon Pyrobaculum islandicum and effects of denaturants and organic solvents., Kujo C, Ohshima T, Appl Environ Microbiol. 1998 Jun;64(6):2152-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9603828 9603828]
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[[Category: Glutamate dehydrogenase]]
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[[Category: Pyrobaculum islandicum]]
[[Category: Pyrobaculum islandicum]]
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[[Category: Single protein]]
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[[Category: Bhuiya MW]]
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[[Category: Bhuiya, M W.]]
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[[Category: Imagawa T]]
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[[Category: Imagawa, T.]]
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[[Category: Katunuma N]]
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[[Category: Katunuma, N.]]
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[[Category: Ohshima T]]
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[[Category: Ohshima, T.]]
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[[Category: Sakuraba H]]
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[[Category: Sakuraba, H.]]
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[[Category: Tsuge H]]
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[[Category: Tsuge, H.]]
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[[Category: Protein-nad complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:33:54 2008''
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Current revision

L-glutamate dehydrogenase from Pyrobaculum islandicum complexed with NAD

PDB ID 1v9l

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