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1cm7

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[[Image:1cm7.jpg|left|200px]]
 
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{{Structure
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==3-ISOPROPYLMALATE DEHYDROGENASE FROM ESCHERICHIA COLI==
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|PDB= 1cm7 |SIZE=350|CAPTION= <scene name='initialview01'>1cm7</scene>, resolution 2.06&Aring;
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<StructureSection load='1cm7' size='340' side='right'caption='[[1cm7]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1cm7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CM7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CM7 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.06&#8491;</td></tr>
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|GENE= LEUB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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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=1cm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cm7 OCA], [https://pdbe.org/1cm7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cm7 RCSB], [https://www.ebi.ac.uk/pdbsum/1cm7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cm7 ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LEU3_ECOLI LEU3_ECOLI] 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/cm/1cm7_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=1cm7 ConSurf].
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<div style="clear:both"></div>
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'''3-ISOPROPYLMALATE DEHYDROGENASE FROM ESCHERICHIA COLI'''
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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 basis of protein stability has been investigated by the structural comparison of themophilic enzymes with their mesophilic counterparts. A number of characteristics have been found that can contribute to the stabilization of thermophilic proteins, but no one is uniquely capable of imparting thermostability. The crystal structure of 3-isopropylmalate dehydrogenase (IPMDH) from the mesophiles Escherichia coli and Salmonella typhimurium have been determined by the method of molecular replacement using the known structure of the homologous Thermus thermophilus enzyme. The structure of the E. coli enzyme was refined at a resolution of 2.1 A to an R-factor of 17.3%, that of the S. typhimurium enzyme at 1.7 A resolution to an R-factor of 19.8%. The three structures were compared to elucidate the basis of the higher thermostability of the T. thermophilus enzyme. A mutant that created a cavity in the hydrophobic core of the thermophilic enzyme was designed to investigate the importance of packing density for thermostability. The structure of this mutant was analyzed. The main stabilizing features in the thermophilic enzyme are an increased number of salt bridges, additional hydrogen bonds, a proportionately larger and more hydrophobic subunit interface, shortened N and C termini and a larger number of proline residues. The mutation in the hydrophobic core of T. thermophilus IPMDH resulted in a cavity of 32 A3, but no significant effect on the activity and thermostability of the mutant was observed.
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==About this Structure==
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1CM7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CM7 OCA].
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==Reference==
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Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus., Wallon G, Kryger G, Lovett ST, Oshima T, Ringe D, Petsko GA, J Mol Biol. 1997 Mar 14;266(5):1016-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9086278 9086278]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kryger, G.]]
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[[Category: Kryger G]]
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[[Category: Lovett, S T.]]
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[[Category: Lovett ST]]
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[[Category: Oshima, T.]]
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[[Category: Oshima T]]
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[[Category: Petsko, G A.]]
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[[Category: Petsko GA]]
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[[Category: Ringe, D.]]
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[[Category: Ringe D]]
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[[Category: Wallon, G.]]
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[[Category: Wallon G]]
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[[Category: dehydrogenase]]
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[[Category: leucine biosynthetic pathway]]
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[[Category: nad-dependant enzyme]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:26:07 2008''
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Current revision

3-ISOPROPYLMALATE DEHYDROGENASE FROM ESCHERICHIA COLI

PDB ID 1cm7

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