1hrd: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1hrd.gif|left|200px]] | [[Image:1hrd.gif|left|200px]] | ||
'''GLUTAMATE DEHYDROGENASE''' | {{Structure | ||
|PDB= 1hrd |SIZE=350|CAPTION= <scene name='initialview01'>1hrd</scene>, resolution 1.96Å | |||
|SITE= | |||
|LIGAND= | |||
|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= | |||
}} | |||
'''GLUTAMATE DEHYDROGENASE''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1HRD is a [ | 1HRD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_symbiosum Clostridium symbiosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRD OCA]. | ||
==Reference== | ==Reference== | ||
The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures., Yip KS, Stillman TJ, Britton KL, Artymiuk PJ, Baker PJ, Sedelnikova SE, Engel PC, Pasquo A, Chiaraluce R, Consalvi V, Structure. 1995 Nov 15;3(11):1147-58. PMID:[http:// | The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures., Yip KS, Stillman TJ, Britton KL, Artymiuk PJ, Baker PJ, Sedelnikova SE, Engel PC, Pasquo A, Chiaraluce R, Consalvi V, Structure. 1995 Nov 15;3(11):1147-58. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8591026 8591026] | ||
[[Category: Clostridium symbiosum]] | [[Category: Clostridium symbiosum]] | ||
[[Category: Glutamate dehydrogenase]] | [[Category: Glutamate dehydrogenase]] | ||
| Line 21: | Line 30: | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''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 11:40:43 2008'' | ||
Revision as of 12:40, 20 March 2008
| |||||||
| , resolution 1.96Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Glutamate dehydrogenase, with EC number 1.4.1.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GLUTAMATE DEHYDROGENASE
OverviewOverview
BACKGROUND: The hyperthermophile Pyrococcus furiosus is one of the most thermostable organisms known, with an optimum growth temperature of 100 degrees C. The proteins from this organism display extreme thermostability. We have undertaken the structure determination of glutamate dehydrogenase from P. furiosus in order to gain further insights into the relationship between molecular structure and thermal stability. RESULTS: The structure of P. furiosus glutamate dehydrogenase, a homohexameric enzyme, has been determined at 2.2 A resolution and compared with the structure of glutamate dehydrogenase from the mesophile Clostridium symbiosum. CONCLUSIONS: Comparison of the structures of these two enzymes has revealed one major difference: the structure of the hyperthermophilic enzyme contains a striking series of ion-pair networks on the surface of the protein subunits and buried at both interdomain and intersubunit interfaces. We propose that the formation of such extended networks may represent a major stabilizing feature associated with the adaptation of enzymes to extreme temperatures.
About this StructureAbout this Structure
1HRD is a Single protein structure of sequence from Clostridium symbiosum. Full crystallographic information is available from OCA.
ReferenceReference
The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures., Yip KS, Stillman TJ, Britton KL, Artymiuk PJ, Baker PJ, Sedelnikova SE, Engel PC, Pasquo A, Chiaraluce R, Consalvi V, Structure. 1995 Nov 15;3(11):1147-58. PMID:8591026
Page seeded by OCA on Thu Mar 20 11:40:43 2008