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2q99

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Revision as of 09:41, 18 October 2017

Crystal Structure of Saccharopine Dehydrogenase from Saccharomyces cerevisiae

Structural highlights

2q99 is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	LYS1 (ATCC 18824)
Activity:	Saccharopine dehydrogenase (NAD(+), L-lysine-forming), with EC number 1.5.1.7
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LYS1_YEAST] Catalyzes the NAD(+)-dependent cleavage of saccharopine to L-lysine and 2-oxoglutarate.

Evolutionary Conservation

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

Publication Abstract from PubMed

The 1.64 A structure of the apoenzyme form of saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae shows the enzyme to be composed of two domains with similar dinucleotide binding folds with a deep cleft at the interface. The structure reveals homology to alanine dehydrogenase, despite low primary sequence similarity. A model of the ternary complex of SDH, NAD, and saccharopine identifies residues Lys77 and Glu122 as potentially important for substrate binding and/or catalysis, consistent with a proton shuttle mechanism. Furthermore, the model suggests that a conformational change is required for catalysis and that residues Lys99 and Asp281 may be instrumental in mediating this change. Analysis of the crystal structure in the context of other homologous enzymes from pathogenic fungi and human sources sheds light into the suitability of SDH as a target for antimicrobial drug development.

Structural studies of the final enzyme in the alpha-aminoadipate pathway-saccharopine dehydrogenase from Saccharomyces cerevisiae.,Burk DL, Hwang J, Kwok E, Marrone L, Goodfellow V, Dmitrienko GI, Berghuis AM J Mol Biol. 2007 Oct 26;373(3):745-54. Epub 2007 Aug 24. PMID:17854830^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Burk DL, Hwang J, Kwok E, Marrone L, Goodfellow V, Dmitrienko GI, Berghuis AM. Structural studies of the final enzyme in the alpha-aminoadipate pathway-saccharopine dehydrogenase from Saccharomyces cerevisiae. J Mol Biol. 2007 Oct 26;373(3):745-54. Epub 2007 Aug 24. PMID:17854830 doi:10.1016/j.jmb.2007.08.044

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2q99"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Saccharopine Dehydrogenase from Saccharomyces cerevisiae==
 <StructureSection load='2q99' size='340' side='right' caption='[[2q99]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LYS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Saccharopine_dehydrogenase_(NAD(+),_L-lysine-forming) Saccharopine dehydrogenase (NAD(+), L-lysine-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.7 1.5.1.7] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q99 OCA], [http://pdbe.org/2q99 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q99 RCSB], [http://www.ebi.ac.uk/pdbsum/2q99 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q99 OCA], [http://pdbe.org/2q99 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q99 RCSB], [http://www.ebi.ac.uk/pdbsum/2q99 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2q99 ProSAT]</span></td></tr>
 </table>
 == Function ==

2q99

From Proteopedia

Revision as of 09:41, 18 October 2017

Crystal Structure of Saccharopine Dehydrogenase from Saccharomyces cerevisiae

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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