2bie: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:2bie.gif|left|200px]]
[[Image:2bie.gif|left|200px]]


{{Structure
<!--
|PDB= 2bie |SIZE=350|CAPTION= <scene name='initialview01'>2bie</scene>, resolution 1.30&Aring;
The line below this paragraph, containing "STRUCTURE_2bie", creates the "Structure Box" on the page.
|SITE= <scene name='pdbsite=AC1:Peg+Binding+Site+For+Chain+B'>AC1</scene>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoserine_transaminase Phosphoserine transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.52 2.6.1.52] </span>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_2bie| PDB=2bie  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bie OCA], [http://www.ebi.ac.uk/pdbsum/2bie PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bie RCSB]</span>
}}


'''RADIATION DAMAGE OF THE SCHIFF BASE IN PHOSPHOSERINE AMINOTRANSFERASE (STRUCTURE H)'''
'''RADIATION DAMAGE OF THE SCHIFF BASE IN PHOSPHOSERINE AMINOTRANSFERASE (STRUCTURE H)'''
Line 30: Line 27:
[[Category: Popov, A N.]]
[[Category: Popov, A N.]]
[[Category: Ravelli, R B.G.]]
[[Category: Ravelli, R B.G.]]
[[Category: aminotransferase]]
[[Category: Aminotransferase]]
[[Category: pyridoxal-5'-phosphate]]
[[Category: Pyridoxal-5'-phosphate]]
[[Category: radiation damage]]
[[Category: Radiation damage]]
[[Category: transferase]]
[[Category: Transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:19:49 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:06:52 2008''

Revision as of 20:19, 3 May 2008

File:2bie.gif

Template:STRUCTURE 2bie

RADIATION DAMAGE OF THE SCHIFF BASE IN PHOSPHOSERINE AMINOTRANSFERASE (STRUCTURE H)


OverviewOverview

The X-ray susceptibility of the lysine-pyridoxal-5'-phosphate Schiff base in Bacillus alcalophilus phosphoserine aminotransferase has been investigated using crystallographic data collected at 100 K to 1.3 A resolution, complemented by on-line spectroscopic studies. X-rays induce deprotonation of the internal aldimine, changes in the Schiff base conformation, displacement of the cofactor molecule, and disruption of the Schiff base linkage between pyridoxal-5'-phosphate and the Lys residue. Analysis of the "undamaged" structure reveals a significant chemical strain on the internal aldimine bond that leads to a pronounced geometrical distortion of the cofactor. However, upon crystal exposure to the X-rays, the strain and distortion are relaxed and eventually diminished when the total absorbed dose has exceeded 4.7 x 10(6) Ggamma. Our data provide new insights into the enzymatic activation of pyridoxal-5'-phosphate and suggest that special care should be taken while using macromolecular crystallography to study details in strained active sites.

About this StructureAbout this Structure

2BIE is a Single protein structure of sequence from Bacillus alcalophilus. Full crystallographic information is available from OCA.

ReferenceReference

Strain relief at the active site of phosphoserine aminotransferase induced by radiation damage., Dubnovitsky AP, Ravelli RB, Popov AN, Papageorgiou AC, Protein Sci. 2005 Jun;14(6):1498-507. Epub 2005 May 9. PMID:15883191 Page seeded by OCA on Sat May 3 20:19:49 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA