1xac: Difference between revisions

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New page: left|200px<br /><applet load="1xac" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xac, resolution 2.1Å" /> '''CHIMERA ISOPROPYLMALA...
 
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[[Image:1xac.gif|left|200px]]<br /><applet load="1xac" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1xac, resolution 2.1&Aring;" />
'''CHIMERA ISOPROPYLMALATE DEHYDROGENASE BETWEEN BACILLUS SUBTILIS (M) AND THERMUS THERMOPHILUS (T) FROM N-TERMINAL: 20% T MIDDLE 20% M RESIDUAL 60% T, MUTATED AT S82R. LOW TEMPERATURE (100K) STRUCTURE.'''<br />


==Overview==
==CHIMERA ISOPROPYLMALATE DEHYDROGENASE BETWEEN BACILLUS SUBTILIS (M) AND THERMUS THERMOPHILUS (T) FROM N-TERMINAL: 20% T MIDDLE 20% M RESIDUAL 60% T, MUTATED AT S82R. LOW TEMPERATURE (100K) STRUCTURE.==
The crystal structures of thermostable enzyme, 3-isopropylmalate, dehydrogenase of Thermus thermophilus (10T) and a chimeric enzyme between, T. thermophilus and Bacillus subtilus with one point mutation (cS82R), were determined at both 100 and 150 K. At the cryogenic condition, the, volume of the unit cell decreased by 5% as a result of a contraction in, the solvent region. Although the overall structures of both enzymes at low, temperature were the same as that of 10T at room temperature, interactions, between two domains and between two subunits in a functional dimer of, cS82R were significantly altered. The decrease in the average temperature, factor of 10T at low temperature and no significant decrease for cS82R, suggested that the structure of the engineered enzyme (cS82R) may have, many conformational substates even at low temperature, while the native, enzyme (10T) at low temperature has a more definite conformation than that, at room temperature. The location of water molecules around the enzyme, molecule and the calculation of the radii of gyration suggested that cS82R, had a weaker hydration than 10T.
<StructureSection load='1xac' size='340' side='right'caption='[[1xac]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1xac]] 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=1XAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XAC 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]] 2.1&#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=1xac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xac OCA], [https://pdbe.org/1xac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xac RCSB], [https://www.ebi.ac.uk/pdbsum/1xac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xac ProSAT]</span></td></tr>
</table>
== Function ==
[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]
== 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/xa/1xac_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=1xac ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1XAC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/3-isopropylmalate_dehydrogenase 3-isopropylmalate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.85 1.1.1.85] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XAC OCA].
*[[Isopropylmalate dehydrogenase|Isopropylmalate dehydrogenase]]
 
__TOC__
==Reference==
</StructureSection>
Cryocrystallography of 3-Isopropylmalate dehydrogenase from Thermus thermophilus and its chimeric enzyme., Nagata C, Moriyama H, Tanaka N, Nakasako M, Yamamoto M, Ueki T, Oshima T, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):623-30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299625 15299625]
[[Category: Large Structures]]
[[Category: 3-isopropylmalate dehydrogenase]]
[[Category: Thermus thermophilus HB8]]
[[Category: Single protein]]
[[Category: Moriyama H]]
[[Category: Thermus thermophilus]]
[[Category: Nagata C]]
[[Category: Moriyama, H.]]
[[Category: Tanaka N]]
[[Category: Nagata, C.]]
[[Category: Tanaka, N.]]
[[Category: chimera]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:56:21 2007''

Latest revision as of 11:48, 14 February 2024

CHIMERA ISOPROPYLMALATE DEHYDROGENASE BETWEEN BACILLUS SUBTILIS (M) AND THERMUS THERMOPHILUS (T) FROM N-TERMINAL: 20% T MIDDLE 20% M RESIDUAL 60% T, MUTATED AT S82R. LOW TEMPERATURE (100K) STRUCTURE.CHIMERA ISOPROPYLMALATE DEHYDROGENASE BETWEEN BACILLUS SUBTILIS (M) AND THERMUS THERMOPHILUS (T) FROM N-TERMINAL: 20% T MIDDLE 20% M RESIDUAL 60% T, MUTATED AT S82R. LOW TEMPERATURE (100K) STRUCTURE.

Structural highlights

1xac is a 1 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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]

Evolutionary Conservation

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

See Also

1xac, resolution 2.10Å

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