1leh

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(New page: 200px<br /><applet load="1leh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1leh, resolution 2.2&Aring;" /> '''LEUCINE DEHYDROGENASE...)
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[[Image:1leh.gif|left|200px]]<br /><applet load="1leh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1leh, resolution 2.2&Aring;" />
 
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'''LEUCINE DEHYDROGENASE FROM BACILLUS SPHAERICUS'''<br />
 
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==Overview==
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==LEUCINE DEHYDROGENASE FROM BACILLUS SPHAERICUS==
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BACKGROUND: Glutamate, phenylalanine and leucine dehydrogenases catalyze, the NAD(P)(+)-linked oxidative deamination of L-amino acids to the, corresponding 2-oxoacids, and sequence homology between these enzymes, clearly indicates the existence of an enzyme superfamily related by, divergent evolution. We have undertaken structural studies on a number of, members of this family in order to investigate the molecular basis of, their differential amino acid specificity. RESULTS: We have solved the, X-ray structure of the leucine dehydrogenase from Bacillus sphaericus to a, resolution of 2.2 A. Each subunit of this octameric enzyme contains 364, amino acids and folds into two domains, separated by a deep cleft. The, nicotinamide ring of the NAD+ cofactor binds deep in this cleft, which is, thought to close during the hydride transfer step of the catalytic cycle., CONCLUSIONS: Comparison of the structure of leucine dehydrogenase with a, hexameric glutamate dehydrogenase has shown that these two enzymes share a, related fold and possess a similar catalytic chemistry. A mechanism for, the basis of the differential amino acid specificity between these enzymes, involves point mutations in the amino acid side-chain specificity pocket, and subtle changes in the shape of this pocket caused by the differences, in quaternary structure.
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<StructureSection load='1leh' size='340' side='right'caption='[[1leh]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1leh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysinibacillus_sphaericus Lysinibacillus sphaericus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LEH FirstGlance]. <br>
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1LEH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lysinibacillus_sphaericus Lysinibacillus sphaericus]. Active as [http://en.wikipedia.org/wiki/Leucine_dehydrogenase Leucine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.9 1.4.1.9] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LEH OCA].
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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]] 2.2&#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=1leh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1leh OCA], [https://pdbe.org/1leh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1leh RCSB], [https://www.ebi.ac.uk/pdbsum/1leh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1leh ProSAT]</span></td></tr>
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==Reference==
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</table>
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A role for quaternary structure in the substrate specificity of leucine dehydrogenase., Baker PJ, Turnbull AP, Sedelnikova SE, Stillman TJ, Rice DW, Structure. 1995 Jul 15;3(7):693-705. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8591046 8591046]
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== Function ==
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[[Category: Leucine dehydrogenase]]
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[https://www.uniprot.org/uniprot/Q7SIB4_LYSSH Q7SIB4_LYSSH]
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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/le/1leh_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=1leh ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Lysinibacillus sphaericus]]
[[Category: Lysinibacillus sphaericus]]
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[[Category: Single protein]]
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[[Category: Baker PJ]]
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[[Category: Baker, P.J.]]
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[[Category: Rice DW]]
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[[Category: Rice, D.W.]]
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[[Category: Sedelnikova SE]]
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[[Category: Sedelnikova, S.E.]]
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[[Category: Stillman TJ]]
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[[Category: Stillman, T.J.]]
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[[Category: Turnbull AP]]
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[[Category: Turnbull, A.P.]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:52:29 2007''
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Current revision

LEUCINE DEHYDROGENASE FROM BACILLUS SPHAERICUS

PDB ID 1leh

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