1v9l
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1v9l.jpg|left|200px]] | + | [[Image:1v9l.jpg|left|200px]] |
| - | + | ||
| - | '''L-glutamate dehydrogenase from Pyrobaculum islandicum complexed with NAD''' | + | {{Structure |
| + | |PDB= 1v9l |SIZE=350|CAPTION= <scene name='initialview01'>1v9l</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Glutamate_dehydrogenase Glutamate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.2 1.4.1.2] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''L-glutamate dehydrogenase from Pyrobaculum islandicum complexed with NAD''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1V9L is a [ | + | 1V9L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_islandicum Pyrobaculum islandicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9L OCA]. |
==Reference== | ==Reference== | ||
| - | The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum., Bhuiya MW, Sakuraba H, Ohshima T, Imagawa T, Katunuma N, Tsuge H, J Mol Biol. 2005 Jan 14;345(2):325-37. PMID:[http:// | + | The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum., Bhuiya MW, Sakuraba H, Ohshima T, Imagawa T, Katunuma N, Tsuge H, J Mol Biol. 2005 Jan 14;345(2):325-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15571725 15571725] |
[[Category: Glutamate dehydrogenase]] | [[Category: Glutamate dehydrogenase]] | ||
[[Category: Pyrobaculum islandicum]] | [[Category: Pyrobaculum islandicum]] | ||
| Line 23: | Line 32: | ||
[[Category: protein-nad complex]] | [[Category: protein-nad complex]] | ||
| - | ''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 14:42:37 2008'' |
Revision as of 12:42, 20 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Glutamate dehydrogenase, with EC number 1.4.1.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
L-glutamate dehydrogenase from Pyrobaculum islandicum complexed with NAD
Overview
The extremely thermostable NAD-dependent glutamate dehydrogenase (NAD-GluDH) from Pyrobaculum islandicum, a member of the Crenarchaeota, was crystallized, and its 3D structure has been determined by X-ray diffraction methods. The homohexameric structure of Pb. islandicum glutamate dehydrogenase (Pis-GluDH) was solved and refined at a resolution of 2.9A with a crystallographic R-factor of 19.9% (Rfree 26.0%). The structure indicates that each subunit consists of two domains separated by a deep cleft containing an active site. The secondary structural elements and catalytically important residues of the enzyme were highly conserved among the NAD(P)-dependent GluDHs from other sources. A structural comparison of Pis-GluDH with other NAD(P)-dependent GluDHs suggests that a significant difference in the alpha8-loop-alpha9 region of this enzyme is associated with its coenzyme specificity. From the analysis of the 3D structure, hydrophobic interactions between intersubunits were found to be important features for the enzyme oligomerization. It has been reported that Pis-GluDH is highly thermostable, like the GluDH of the hyperthermophilic archaeum Pyrococcus furiosus, and the increase in the intersubunit ion pair networks is responsible for the extreme thermostability of the Pc. furiosus enzyme. However, the number of intersubunit ion pairs in the Pis-GluDH molecules is much smaller than those of the Pc. furiosus GluDH. The number of hydrophobic interactions at the intersubunit interfaces were increased and responsible for the extremely high thermostability. This indicates that the major molecular strategy for high thermostability of the GluDHs may be different for each hyperthermophile.
About this Structure
1V9L is a Single protein structure of sequence from Pyrobaculum islandicum. Full crystallographic information is available from OCA.
Reference
The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum., Bhuiya MW, Sakuraba H, Ohshima T, Imagawa T, Katunuma N, Tsuge H, J Mol Biol. 2005 Jan 14;345(2):325-37. PMID:15571725
Page seeded by OCA on Thu Mar 20 14:42:37 2008
