1zem
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1zem |SIZE=350|CAPTION= <scene name='initialview01'>1zem</scene>, resolution 1.9Å | |PDB= 1zem |SIZE=350|CAPTION= <scene name='initialview01'>1zem</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/D-xylulose_reductase D-xylulose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.9 1.1.1.9] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/D-xylulose_reductase D-xylulose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.9 1.1.1.9] </span> |
|GENE= AB091690 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=442 Gluconobacter oxydans]) | |GENE= AB091690 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=442 Gluconobacter oxydans]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zem OCA], [http://www.ebi.ac.uk/pdbsum/1zem PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zem RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Elling, R A.]] | [[Category: Elling, R A.]] | ||
[[Category: Wilson, D K.]] | [[Category: Wilson, D K.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: NAD]] | ||
[[Category: dinucleotide-binding domain]] | [[Category: dinucleotide-binding domain]] | ||
[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:34:57 2008'' |
Revision as of 22:35, 30 March 2008
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | AB091690 (Gluconobacter oxydans) | ||||||
| Activity: | D-xylulose reductase, with EC number 1.1.1.9 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of NAD+-Bound Xylitol Dehydrogenase
Overview
Xylitol dehydrogenase (XDH) is one of several enzymes responsible for assimilating xylose into eukaryotic metabolism and is useful for fermentation of xylose contained in agricultural byproducts to produce ethanol. For efficient xylose utilization at high flux rates, cosubstrates should be recycled between the NAD+-specific XDH and the NADPH-preferring xylose reductase, another enzyme in the pathway. To understand and alter the cosubstrate specificity of XDH, we determined the crystal structure of the Gluconobacter oxydans holoenzyme to 1.9 angstroms resolution. The structure reveals that NAD+ specificity is largely conferred by Asp38, which interacts with the hydroxyls of the adenosine ribose. Met39 stacked under the purine ring and was also located near the 2' hydroxyl. Based on the location of these residues and on sequence alignments with related enzymes of various cosubstrate specificities, we constructed a double mutant (D38S/M39R) that was able to exclusively use NADP+, with no loss of activity.
About this Structure
1ZEM is a Single protein structure of sequence from Gluconobacter oxydans. Full crystallographic information is available from OCA.
Reference
Structure-guided engineering of xylitol dehydrogenase cosubstrate specificity., Ehrensberger AH, Elling RA, Wilson DK, Structure. 2006 Mar;14(3):567-75. PMID:16531240
Page seeded by OCA on Mon Mar 31 01:34:57 2008
