1gde
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1gde |SIZE=350|CAPTION= <scene name='initialview01'>1gde</scene>, resolution 1.8Å | |PDB= 1gde |SIZE=350|CAPTION= <scene name='initialview01'>1gde</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene> | + | |LIGAND= <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1dju|1DJU]], [[1gd9|1GD9]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gde OCA], [http://www.ebi.ac.uk/pdbsum/1gde PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gde RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Matsui, I.]] | [[Category: Matsui, I.]] | ||
[[Category: Ura, H.]] | [[Category: Ura, H.]] | ||
| - | [[Category: GLU]] | ||
| - | [[Category: PLP]] | ||
[[Category: aminotransferase]] | [[Category: aminotransferase]] | ||
[[Category: pyridoxal enzyme]] | [[Category: pyridoxal enzyme]] | ||
[[Category: temperature dependence of substrate recognition]] | [[Category: temperature dependence of substrate recognition]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:41:50 2008'' |
Revision as of 17:41, 30 March 2008
| |||||||
| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1DJU, 1GD9
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF PYROCOCCUS PROTEIN A-1 E-FORM
Overview
We determined the crystal structure of the liganded form of alpha-aminotransferase from a hyperthermophile, Pyrococcus horikoshii. This hyperthermophilic enzyme did not show domain movement upon binding of an acidic substrate, glutamate, except for a small movement of the alpha-helix from Glu16 to Ala25. The omega-carboxyl group of the acidic substrate was recognized by Tyr70* without its side-chain movement, but not by positively charged Arg or Lys. Compared with the homologous enzymes from Thermus thermophilus HB8 and Escherichia coli, it was suggested that the more thermophilic the enzyme is, the smaller the domain movement is. This rule seems to be applicable to many other enzymes already reported.
About this Structure
1GDE is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.
Reference
Temperature dependence of the enzyme-substrate recognition mechanism., Ura H, Harata K, Matsui I, Kuramitsu S, J Biochem. 2001 Jan;129(1):173-8. PMID:11134972
Page seeded by OCA on Sun Mar 30 20:41:50 2008
