1dds: Difference between revisions

Revision as of 13:44, 2 May 2008

MOLECULE: DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH METHOTREXATE

OverviewOverview

Virtually all studies of the protein-folding reaction add either heat, acid, or a chemical denaturant to an aqueous protein solution in order to perturb the protein structure. When chemical denaturants are used, very high concentrations are usually necessary to observe any change in protein structure. In a solution with such high denaturant concentrations, both the structure of the protein and the structure of the solvent around the protein can be altered. X-ray crystallography is the obvious experimental technique to probe both types of changes. In this paper, we report the crystal structures of dihydrofolate reductase with urea and of ribonuclease A with guanidinium chloride. These two classic denaturants have similar effects on the native structure of the protein. The most important change that occurs is a reduction in the overall thermal factor. These structures offer a molecular explanation for the reduction in mobility. Although the reduction is observed only with the native enzyme in the crystal, a similar decrease in mobility has also been observed in the unfolded state in solution (Makhatadze G, Privalov PL. 1992. Protein interactions with urea and guanidinium chloride: A calorimetric study.

About this StructureAbout this Structure

1DDS is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

The effect of denaturants on protein structure., Dunbar J, Yennawar HP, Banerjee S, Luo J, Farber GK, Protein Sci. 1997 Aug;6(8):1727-33. PMID:9260285 Page seeded by OCA on Fri May 2 13:44:16 2008

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

OCA

@@ Line 1: / Line 1: @@
 [[Image:1dds.gif|left|200px]]
- {{Structure
+<!--
-|PDB= 1dds |SIZE=350|CAPTION= <scene name='initialview01'>1dds</scene>, resolution 2.2&Aring;
+The line below this paragraph, containing "STRUCTURE_1dds", creates the "Structure Box" on the page.
-|SITE=
+You may change the PDB parameter (which sets the PDB file loaded into the applet)
-|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MTX:METHOTREXATE'>MTX</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/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </span>
+or leave the SCENE parameter empty for the default display.
-|GENE=
+-->
-|DOMAIN=
+{{STRUCTURE_1dds|  PDB=1dds  |  SCENE=  }}
-|RELATEDENTRY=
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dds OCA], [http://www.ebi.ac.uk/pdbsum/1dds PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dds RCSB]</span>
-}}
 '''MOLECULE: DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH METHOTREXATE'''
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 [[Category: Farber, G K.]]
 [[Category: Yennawar, H P.]]
-[[Category: oxido-reductase]]
+[[Category: Oxido-reductase]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:44:16 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:39:37 2008''