1leh: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<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>
<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>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Leucine_dehydrogenase Leucine dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.9 1.4.1.9] </span></td></tr>
</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>
<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>
<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>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q7SIB4_LYSSH Q7SIB4_LYSSH]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:8591046<ref>PMID:8591046</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1leh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Leucine dehydrogenase]]
[[Category: Lysinibacillus sphaericus]]
[[Category: Lysinibacillus sphaericus]]
[[Category: Baker, P J]]
[[Category: Baker PJ]]
[[Category: Rice, D W]]
[[Category: Rice DW]]
[[Category: Sedelnikova, S E]]
[[Category: Sedelnikova SE]]
[[Category: Stillman, T J]]
[[Category: Stillman TJ]]
[[Category: Turnbull, A P]]
[[Category: Turnbull AP]]
[[Category: Oxidoreductase]]
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