1nsy
From Proteopedia
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| - | [[Image:1nsy.gif|left|200px]] | + | [[Image:1nsy.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF NH3-DEPENDENT NAD+ SYNTHETASE FROM BACILLUS SUBTILIS''' | + | {{Structure |
| + | |PDB= 1nsy |SIZE=350|CAPTION= <scene name='initialview01'>1nsy</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene> and <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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF NH3-DEPENDENT NAD+ SYNTHETASE FROM BACILLUS SUBTILIS''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NSY is a [ | + | 1NSY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NSY OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8895556 8895556] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: NAD(+) synthase (glutamine-hydrolyzing)]] | [[Category: NAD(+) synthase (glutamine-hydrolyzing)]] | ||
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[[Category: nh3 dependent]] | [[Category: nh3 dependent]] | ||
| - | ''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 13:01:19 2008'' |
Revision as of 11:01, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | , , and | ||||||
| Activity: | NAD(+) synthase (glutamine-hydrolyzing), with EC number 6.3.5.1 | ||||||
| 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
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