1g2u

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[[Image:1g2u.jpg|left|200px]]
 
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==THE STRUCTURE OF THE MUTANT, A172V, OF 3-ISOPROPYLMALATE DEHYDROGENASE FROM THERMUS THERMOPHILUS HB8 : ITS THERMOSTABILITY AND STRUCTURE.==
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The line below this paragraph, containing "STRUCTURE_1g2u", creates the "Structure Box" on the page.
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<StructureSection load='1g2u' size='340' side='right'caption='[[1g2u]], [[Resolution|resolution]] 2.10&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'>[[1g2u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G2U 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]] 2.1&#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=1g2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g2u OCA], [https://pdbe.org/1g2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g2u RCSB], [https://www.ebi.ac.uk/pdbsum/1g2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g2u ProSAT]</span></td></tr>
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{{STRUCTURE_1g2u| PDB=1g2u | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LEU3_THET8 LEU3_THET8] Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.[HAMAP-Rule:MF_01033]
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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/g2/1g2u_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=1g2u ConSurf].
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<div style="clear:both"></div>
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'''THE STRUCTURE OF THE MUTANT, A172V, OF 3-ISOPROPYLMALATE DEHYDROGENASE FROM THERMUS THERMOPHILUS HB8 : ITS THERMOSTABILITY AND STRUCTURE.'''
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==See Also==
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*[[Isopropylmalate dehydrogenase|Isopropylmalate dehydrogenase]]
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__TOC__
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==Overview==
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</StructureSection>
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The relationship between the structure and the thermostability of the 3-isopropylmalate dehydrogenase from Thermus thermophilus was studied by site-directed mutation of a single Ala residue located at the domain interface. The crystal structures of three mutant enzymes, replacing Ala172 with Gly, Val and Phe, were successfully determined at 2.3, 2.2 and 2.5 A resolution, respectively. Substitution of Ala172 by relatively 'short' residues (Gly, Val or Ile) enlarges or narrows the cavity in the vicinity of the C(beta) atom of Ala172 and the thermostablity of the enzyme shows a good correlation with the hydrophobicity of the substituted residues. Substitution of Ala172 by the 'longer' residues Leu or Phe causes a rearrangement of the domain structure, which leads to a higher thermostability of the enzymes than that expected from the hydrophobicity of the substituted residues. Mutation of Ala172 to negatively charged residues gave an unexpected result: the melting temperature of the Asp mutant enzyme was reduced by 2.7 K while that of the Glu mutant increased by 1.8 K. Molecular-modelling studies indicated that the glutamate side chain was sufficiently long that it did not act as a buried charge as did the aspartate, but instead protruded to the outside of the hydrophobic cavity and contributed to the stability of the enzyme by enhancing the packing of the local side chains and forming an extra salt bridge with the side chain of Lys175.
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[[Category: Large Structures]]
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[[Category: Thermus thermophilus HB8]]
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==About this Structure==
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[[Category: Akanuma S]]
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1G2U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G2U OCA].
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[[Category: Moriyama H]]
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[[Category: Oshima T]]
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==Reference==
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[[Category: Qu C]]
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Design, X-ray crystallography, molecular modelling and thermal stability studies of mutant enzymes at site 172 of 3-isopropylmalate dehydrogenase from Thermus thermophilus., Qu C, Akanuma S, Tanaka N, Moriyama H, Oshima T, Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):225-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11173468 11173468]
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[[Category: Tanaka N]]
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[[Category: 3-isopropylmalate dehydrogenase]]
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[[Category: Single protein]]
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[[Category: Thermus thermophilus]]
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[[Category: Akanuma, S.]]
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[[Category: Moriyama, H.]]
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[[Category: Oshima, T.]]
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[[Category: Qu, C.]]
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[[Category: Tanaka, N.]]
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[[Category: Beta-barrel]]
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[[Category: Nad binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:04:12 2008''
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Current revision

THE STRUCTURE OF THE MUTANT, A172V, OF 3-ISOPROPYLMALATE DEHYDROGENASE FROM THERMUS THERMOPHILUS HB8 : ITS THERMOSTABILITY AND STRUCTURE.

PDB ID 1g2u

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