1w85: Difference between revisions

Revision as of 13:17, 3 May 2008

THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1 BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2

OverviewOverview

Thiamine diphosphate (ThDP) is used as a cofactor in many key metabolic enzymes. We present evidence that the ThDPs in the two active sites of the E1 (EC 1.2.4.1) component of the pyruvate dehydrogenase complex communicate over a distance of 20 angstroms by reversibly shuttling a proton through an acidic tunnel in the protein. This "proton wire" permits the co-factors to serve reciprocally as general acid/base in catalysis and to switch the conformation of crucial active-site peptide loops. This synchronizes the progression of chemical events and can account for the oligomeric organization, conformational asymmetry, and "ping-pong" kinetic properties of E1 and other thiamine-dependent enzymes.

About this StructureAbout this Structure

1W85 is a Protein complex structure of sequences from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

ReferenceReference

A molecular switch and proton wire synchronize the active sites in thiamine enzymes., Frank RA, Titman CM, Pratap JV, Luisi BF, Perham RN, Science. 2004 Oct 29;306(5697):872-6. PMID:15514159 Page seeded by OCA on Sat May 3 13:17:26 2008

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

OCA

@@ Line 1: / Line 1: @@
 [[Image:1w85.gif|left|200px]]
- {{Structure
+<!--
-|PDB= 1w85 |SIZE=350|CAPTION= <scene name='initialview01'>1w85</scene>, resolution 2.00&Aring;
+The line below this paragraph, containing "STRUCTURE_1w85", creates the "Structure Box" on the page.
-|SITE= <scene name='pdbsite=AC1:Tdp+Binding+Site+For+Chain+G'>AC1</scene>
+You may change the PDB parameter (which sets the PDB file loaded into the applet)
-|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TDP:THIAMIN+DIPHOSPHATE'>TDP</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/Pyruvate_dehydrogenase_(acetyl-transferring) Pyruvate dehydrogenase (acetyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.1 1.2.4.1] </span>
+or leave the SCENE parameter empty for the default display.
-|GENE=
+-->
-|DOMAIN=
+{{STRUCTURE_1w85|  PDB=1w85  |  SCENE=  }}
-|RELATEDENTRY=
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w85 OCA], [http://www.ebi.ac.uk/pdbsum/1w85 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w85 RCSB]</span>
-}}
 '''THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1 BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2'''
@@ Line 25: / Line 22: @@
 [[Category: Geobacillus stearothermophilus]]
 [[Category: Protein complex]]
-[[Category: Pyruvate dehydrogenase (acetyl-transferring)]]
 [[Category: Frank, R A.W.]]
 [[Category: Luisi, B F.]]
@@ Line 31: / Line 27: @@
 [[Category: Perham, R N.]]
 [[Category: Pratap, J V.]]
-[[Category: acetyl transferase]]
+[[Category: Acetyl transferase]]
-[[Category: dehydrogenase]]
+[[Category: Dehydrogenase]]
-[[Category: dihydrolipoyl]]
+[[Category: Dihydrolipoyl]]
-[[Category: multienzyme complex]]
+[[Category: Multienzyme complex]]
-[[Category: oxidoreductase]]
+[[Category: Oxidoreductase]]
-[[Category: pyruvate]]
+[[Category: Pyruvate]]
-[[Category: transferase]]
+[[Category: Transferase]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:17:26 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:32:32 2008''