1s20
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1s20 |SIZE=350|CAPTION= <scene name='initialview01'>1s20</scene>, resolution 2.20Å | |PDB= 1s20 |SIZE=350|CAPTION= <scene name='initialview01'>1s20</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= YIAK, B3575 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= YIAK, B3575 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1nxu|1NXU]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s20 OCA], [http://www.ebi.ac.uk/pdbsum/1s20 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s20 RCSB]</span> | ||
}} | }} | ||
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[[Category: Tong, L.]] | [[Category: Tong, L.]] | ||
[[Category: Xiao, R.]] | [[Category: Xiao, R.]] | ||
| - | [[Category: NAD]] | ||
| - | [[Category: TLA]] | ||
[[Category: alpha beta dimeric protein]] | [[Category: alpha beta dimeric protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:36:13 2008'' |
Revision as of 20:36, 30 March 2008
| |||||||
| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | YIAK, B3575 (Escherichia coli) | ||||||
| Related: | 1NXU
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
A novel NAD binding protein revealed by the crystal structure of E. Coli 2,3-diketogulonate reductase (YiaK)
Overview
Escherichia coli YiaK catalyzes the reduction of 2,3-diketo-L-gulonate in the presence of NADH. It belongs to a large family of oxidoreductases that is conserved in archaea, bacteria, and eukaryotes but shows no sequence homology to other proteins. We report here the crystal structures at up to 2.0-A resolution of YiaK alone and in complex with NAD-tartrate. YiaK has a new polypeptide backbone fold and a novel mode of recognizing the NAD cofactor. In addition, NAD is bound in an unusual conformation, at the interface of a dimer of the enzyme. The crystallographic analysis unexpectedly revealed the binding of tartrate in the active site. Enzyme kinetics studies confirm that tartrate and the related D-malate are inhibitors of YiaK. In contrast to most other enzymes where substrate binding produces a more closed conformation, the binding of NAD-tartrate to YiaK produces a more open active site. The free enzyme conformation is incompatible with NAD binding. His(44) is likely the catalytic residue of the enzyme.
About this Structure
1S20 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
A novel NAD-binding protein revealed by the crystal structure of 2,3-diketo-L-gulonate reductase (YiaK)., Forouhar F, Lee I, Benach J, Kulkarni K, Xiao R, Acton TB, Montelione GT, Tong L, J Biol Chem. 2004 Mar 26;279(13):13148-55. Epub 2004 Jan 12. PMID:14718529
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