1nsy
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1nsy |SIZE=350|CAPTION= <scene name='initialview01'>1nsy</scene>, resolution 2.0Å | |PDB= 1nsy |SIZE=350|CAPTION= <scene name='initialview01'>1nsy</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/NAD(+)_synthase_(glutamine-hydrolyzing) NAD(+) synthase (glutamine-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.1 6.3.5.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_synthase_(glutamine-hydrolyzing) NAD(+) synthase (glutamine-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.1 6.3.5.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nsy OCA], [http://www.ebi.ac.uk/pdbsum/1nsy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nsy RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Nessi, C.]] | [[Category: Nessi, C.]] | ||
[[Category: Rizzi, M.]] | [[Category: Rizzi, M.]] | ||
| - | [[Category: AMP]] | ||
| - | [[Category: ATP]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: POP]] | ||
[[Category: amidotransferase]] | [[Category: amidotransferase]] | ||
[[Category: atp pyrophosphatase]] | [[Category: atp pyrophosphatase]] | ||
| Line 37: | Line 36: | ||
[[Category: nh3 dependent]] | [[Category: nh3 dependent]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:35:07 2008'' |
Revision as of 19:35, 30 March 2008
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | NAD(+) synthase (glutamine-hydrolyzing), with EC number 6.3.5.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF NH3-DEPENDENT NAD+ SYNTHETASE FROM BACILLUS SUBTILIS
Overview
NAD+ synthetase catalyzes the last step in the biosynthesis of nicotinamide adenine dinucleotide. The three-dimensional structure of NH3-dependent NAD+ synthetase from Bacillus subtilis, in its free form and in complex with ATP, has been solved by X-ray crystallography (at 2.6 and 2.0 angstroms resolution, respectively) using a combination of multiple isomorphous replacement and density modification techniques. The enzyme consists of a tight homodimer with alpha/beta subunit topology. The catalytic site is located at the parallel beta-sheet topological switch point, where one AMP molecule, one pyrophosphate and one Mg2+ ion are observed. Residue Ser46, part of the neighboring 'P-loop', is hydrogen bonded to the pyrophosphate group, and may play a role in promoting the adenylation of deamido-NAD+ during the first step of the catalyzed reaction. The deamido-NAD+ binding site, located at the subunit interface, is occupied by one ATP molecule, pointing towards the catalytic center. A conserved structural fingerprint of the catalytic site, comprising Ser46, is very reminiscent of a related protein region observed in glutamine-dependent GMP synthetase, supporting the hypothesis that NAD+ synthetase belongs to the newly discovered family of 'N-type' ATP pyrophosphatases.
About this Structure
1NSY is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis., Rizzi M, Nessi C, Mattevi A, Coda A, Bolognesi M, Galizzi A, EMBO J. 1996 Oct 1;15(19):5125-34. PMID:8895556
Page seeded by OCA on Sun Mar 30 22:35:07 2008
