1ifx
From Proteopedia
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|PDB= 1ifx |SIZE=350|CAPTION= <scene name='initialview01'>1ifx</scene>, resolution 2.25Å | |PDB= 1ifx |SIZE=350|CAPTION= <scene name='initialview01'>1ifx</scene>, resolution 2.25Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=DND:NICOTINIC ACID ADENINE DINUCLEOTIDE'>DND</scene> | + | |LIGAND= <scene name='pdbligand=DND:NICOTINIC+ACID+ADENINE+DINUCLEOTIDE'>DND</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= NadE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= NadE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ee1|1ee1]], [[1fyd|1fyd]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ifx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ifx OCA], [http://www.ebi.ac.uk/pdbsum/1ifx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ifx RCSB]</span> | ||
}} | }} | ||
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[[Category: Singh, R.]] | [[Category: Singh, R.]] | ||
[[Category: Symersky, J.]] | [[Category: Symersky, J.]] | ||
| - | [[Category: DND]] | ||
[[Category: amidotransferase]] | [[Category: amidotransferase]] | ||
[[Category: atp]] | [[Category: atp]] | ||
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[[Category: pyrophosphatase]] | [[Category: pyrophosphatase]] | ||
| - | ''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 21:19:15 2008'' |
Revision as of 18:19, 30 March 2008
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| , resolution 2.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | NadE (Bacillus subtilis) | ||||||
| Activity: | NAD(+) synthase (glutamine-hydrolyzing), with EC number 6.3.5.1 | ||||||
| Related: | 1ee1, 1fyd
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF NH3-DEPENDENT NAD+ SYNTHETASE FROM BACILLUS SUBTILIS COMPLEXED WITH TWO MOLECULES DEAMIDO-NAD
Overview
The NH(3)-dependent NAD(+) synthetase (NADS) participates in the biosynthesis of nicotinamide adenine dinucleotide (NAD(+)) by transforming nicotinic acid adenine dinucleotide (NaAD) to NAD(+). The structural behavior of the active site, including stabilization of flexible loops 82-87 and 204-225, has been studied by determination of the crystal structures of complexes of NADS with natural substrates and a substrate analog. Both loops are stabilized independently of NaAD and solely from the ATP-binding site. Analysis of the binding contacts suggests that the minor loop 82-87 is stabilized primarily by a hydrogen bond with the adenine base of ATP. Formation of a coordination complex with Mg(2+) in the ATP-binding site may contribute to the stabilization of the major loop 204-225. The major loop has a role in substrate recognition and stabilization, in addition to the protection of the reaction intermediate described previously. A second and novel Mg(2+) position has been observed closer to the NaAD-binding site in the structure crystallized at pH 7.5, where the enzyme is active. This could therefore be the catalytically active Mg(2+).
About this Structure
1IFX is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Stabilization of active-site loops in NH3-dependent NAD+ synthetase from Bacillus subtilis., Devedjiev Y, Symersky J, Singh R, Jedrzejas M, Brouillette C, Brouillette W, Muccio D, Chattopadhyay D, DeLucas L, Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):806-12. Epub 2001, May 25. PMID:11375500
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