1k89

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[[Image:1k89.jpg|left|200px]]
 
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==K89L MUTANT OF GLUTAMATE DEHYDROGENASE==
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The line below this paragraph, containing "STRUCTURE_1k89", creates the "Structure Box" on the page.
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<StructureSection load='1k89' size='340' side='right'caption='[[1k89]], [[Resolution|resolution]] 2.05&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'>[[1k89]] is a 1 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=1K89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K89 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]] 2.05&#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=1k89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k89 OCA], [https://pdbe.org/1k89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k89 RCSB], [https://www.ebi.ac.uk/pdbsum/1k89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k89 ProSAT]</span></td></tr>
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{{STRUCTURE_1k89| PDB=1k89 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DHE2_CLOSY DHE2_CLOSY]
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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/k8/1k89_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=1k89 ConSurf].
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<div style="clear:both"></div>
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'''K89L MUTANT OF GLUTAMATE DEHYDROGENASE'''
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==See Also==
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*[[Glutamate dehydrogenase 3D structures|Glutamate dehydrogenase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Comparisons of the structures of glutamate dehydrogenase (GluDH) and leucine dehydrogenase (LeuDH) have suggested that two substitutions, deep within the amino acid binding pockets of these homologous enzymes, from hydrophilic residues to hydrophobic ones are critical components of their differential substrate specificity. When one of these residues, K89, which hydrogen-bonds to the gamma-carboxyl group of the substrate l-glutamate in GluDH, was altered by site-directed mutagenesis to a leucine residue, the mutant enzyme showed increased substrate activity for methionine and norleucine but negligible activity with either glutamate or leucine. In order to understand the molecular basis of this shift in specificity we have determined the crystal structure of the K89L mutant of GluDH from Clostridium symbiosum. Analysis of the structure suggests that further subtle differences in the binding pocket prevent the mutant from using a branched hydrophobic substrate but permit the straight-chain amino acids to be used as substrates.The three-dimensional crystal structure of the GluDH from C. symbiosum has been previously determined in two distinct forms in the presence and absence of its substrate glutamate. A comparison of these two structures has revealed that the enzyme can adopt different conformations by flexing about the cleft between its two domains, providing a motion which is critical for orienting the partners involved in the hydride transfer reaction. It has previously been proposed that this conformational change is triggered by substrate binding. However, analysis of the K89L mutant shows that it adopts an almost identical conformation with that of the wild-type enzyme in the presence of substrate. Comparison of the mutant structure with both the wild-type open and closed forms has enabled us to separate conformational changes associated with substrate binding and domain motion and suggests that the domain closure may well be a property of the wild-type enzyme even in the absence of substrate.
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[[Category: Large Structures]]
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[[Category: Baker PJ]]
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==About this Structure==
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[[Category: Britton KL]]
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1K89 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_symbiosum Clostridium symbiosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K89 OCA].
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[[Category: Engel PC]]
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[[Category: Migueis AMB]]
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==Reference==
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[[Category: Rice DW]]
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Insights into the mechanism of domain closure and substrate specificity of glutamate dehydrogenase from Clostridium symbiosum., Stillman TJ, Migueis AM, Wang XG, Baker PJ, Britton KL, Engel PC, Rice DW, J Mol Biol. 1999 Jan 15;285(2):875-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9878450 9878450]
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[[Category: Stillman TJ]]
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[[Category: Clostridium symbiosum]]
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[[Category: Wang XG]]
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[[Category: Glutamate dehydrogenase]]
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[[Category: Single protein]]
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[[Category: Baker, P J.]]
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[[Category: Britton, K L.]]
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[[Category: Engel, P C.]]
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[[Category: Migueis, A M.B.]]
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[[Category: Rice, D W.]]
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[[Category: Stillman, T J.]]
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[[Category: Wang, X G.]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:25:30 2008''
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Current revision

K89L MUTANT OF GLUTAMATE DEHYDROGENASE

PDB ID 1k89

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