2pz8
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2pz8 |SIZE=350|CAPTION= <scene name='initialview01'>2pz8</scene>, resolution 2.00Å | |PDB= 2pz8 |SIZE=350|CAPTION= <scene name='initialview01'>2pz8</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/NAD(+)_synthase NAD(+) synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.5 6.3.1.5] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_synthase NAD(+) synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.5 6.3.1.5] </span> |
|GENE= nadE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 Bacillus anthracis]) | |GENE= nadE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 Bacillus anthracis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2pza|2PZA]], [[2pzb|2PZB]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pz8 OCA], [http://www.ebi.ac.uk/pdbsum/2pz8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pz8 RCSB]</span> | ||
}} | }} | ||
| Line 31: | Line 34: | ||
[[Category: Protasevich, I I.]] | [[Category: Protasevich, I I.]] | ||
[[Category: Pruett, P S.]] | [[Category: Pruett, P S.]] | ||
| - | [[Category: APC]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: MG]] | ||
[[Category: his-tag]] | [[Category: his-tag]] | ||
[[Category: ligase]] | [[Category: ligase]] | ||
[[Category: protein-substrate analog complex]] | [[Category: protein-substrate analog complex]] | ||
| - | ''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 04:42:35 2008'' |
Revision as of 01:42, 31 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | nadE (Bacillus anthracis) | ||||||
| Activity: | NAD(+) synthase, with EC number 6.3.1.5 | ||||||
| Related: | 2PZA, 2PZB
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NAD+ Synthetase from Bacillus anthracis with AMP-CPP and Mg2+
Overview
The crystal structures of NH(3)-dependent NAD+ synthetase from Bacillus anthracis as the apoenzyme (1.9 A), in complex with the natural catalytic products AMP and pyrophosphate (2.4 A) and in complex with the substrate analog adenosine 5'-(alpha,beta-methylene)triphosphate (2.0 A) have been determined. NAD+ synthetase catalyzes the last step in the biosynthesis of the vitally important cofactor NAD+. In comparison to other NAD+ synthetase crystal structures, the C-terminal His-tagged end of the apoenzyme adopts a novel helical conformation, causing significant compensatory changes in the region. The structural accommodations observed in B. anthracis NAD+ synthetase are remarkable in the absence of adverse affects on enzyme activity. They also illustrate a rare example of the influence of a non-native C-terminal His-tag extension on the structure of a native protein. In contrast to the apoenzyme, when AMP and pyrophosphate or adenosine 5'-(alpha,beta-methylene)triphosphate are bound, the C-terminus adopts a conformation that allows ATP binding and overall the structure then resembles other NAD+ synthetase structures. The structures of NAD+ synthetase complexes from B. anthracis are compared with published X-ray crystal structures of the enzyme from B. subtilis, Escherichia coli and Helicobacter pylori. These comparisons support the novel observation that P1 and P2 loop ordering is not a consequence of crystal contacts but rather a consequence of intrinsic intramolecular interactions within the ordered subunit.
About this Structure
2PZ8 is a Single protein structure of sequence from Bacillus anthracis. Full crystallographic information is available from OCA.
Reference
Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD+ synthetase from Bacillus anthracis., McDonald HM, Pruett PS, Deivanayagam C, Protasevich II, Carson WM, DeLucas LJ, Brouillette WJ, Brouillette CG, Acta Crystallogr D Biol Crystallogr. 2007 Aug;63(Pt 8):891-905. Epub 2007, Jul 17. PMID:17642516
Page seeded by OCA on Mon Mar 31 04:42:35 2008
