1cm7: Difference between revisions

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New page: left|200px<br /><applet load="1cm7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cm7, resolution 2.06Å" /> '''3-ISOPROPYLMALATE DE...
 
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'''3-ISOPROPYLMALATE DEHYDROGENASE FROM ESCHERICHIA COLI'''<br />


==Overview==
==3-ISOPROPYLMALATE DEHYDROGENASE FROM ESCHERICHIA COLI==
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.
<StructureSection load='1cm7' size='340' side='right'caption='[[1cm7]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Function ==
[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]
== 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/cm/1cm7_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=1cm7 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1CM7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CM7 OCA].
*[[Isopropylmalate dehydrogenase|Isopropylmalate dehydrogenase]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9086278 9086278]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Kryger, G.]]
[[Category: Kryger G]]
[[Category: Lovett, S.T.]]
[[Category: Lovett ST]]
[[Category: Oshima, T.]]
[[Category: Oshima T]]
[[Category: Petsko, G.A.]]
[[Category: Petsko GA]]
[[Category: Ringe, D.]]
[[Category: Ringe D]]
[[Category: Wallon, G.]]
[[Category: Wallon G]]
[[Category: dehydrogenase]]
[[Category: leucine biosynthetic pathway]]
[[Category: nad-dependant enzyme]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:34:31 2007''

Latest revision as of 08:57, 3 April 2024

3-ISOPROPYLMALATE DEHYDROGENASE FROM ESCHERICHIA COLI3-ISOPROPYLMALATE DEHYDROGENASE FROM ESCHERICHIA COLI

Structural highlights

1cm7 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.06Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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]

Evolutionary Conservation

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

See Also

1cm7, resolution 2.06Å

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