1leh
From Proteopedia
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| - | [[Image:1leh.gif|left|200px]] | + | [[Image:1leh.gif|left|200px]] |
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| - | '''LEUCINE DEHYDROGENASE FROM BACILLUS SPHAERICUS''' | + | {{Structure |
| + | |PDB= 1leh |SIZE=350|CAPTION= <scene name='initialview01'>1leh</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''LEUCINE DEHYDROGENASE FROM BACILLUS SPHAERICUS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LEH is a [ | + | 1LEH is a [[Single protein]] structure of sequence from [http://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]. |
==Reference== | ==Reference== | ||
| - | 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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/8591046 8591046] |
[[Category: Leucine dehydrogenase]] | [[Category: Leucine dehydrogenase]] | ||
[[Category: Lysinibacillus sphaericus]] | [[Category: Lysinibacillus sphaericus]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:29:59 2008'' |
Revision as of 10:30, 20 March 2008
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| , resolution 2.2Å | |||||||
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| Activity: | Leucine dehydrogenase, with EC number 1.4.1.9 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
LEUCINE DEHYDROGENASE FROM BACILLUS SPHAERICUS
Overview
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.
About this Structure
1LEH is a Single protein structure of sequence from Lysinibacillus sphaericus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 12:29:59 2008
