1art: Difference between revisions

Revision as of 10:37, 2 May 2008

X-RAY CRYSTALLOGRAPHIC STUDY OF PYRIDOXAL 5'-PHOSPHATE-TYPE ASPARTATE AMINOTRANSFERASES FROM ESCHERICHIA COLI IN OPEN AND CLOSED FORM

OverviewOverview

We determined the three-dimensional structures of aspartate aminotransferase (AspAT) from Escherichia coli and its complex with inhibitor (2-methyl-L-aspartate) at 1.8A resolution. This enzyme reversibly catalyzes the transamination reaction and is a dimer of two identical subunits. Each subunit has 396 amino acid residues and one pyridoxal 5'-phosphate as a cofactor, and is divided into two domains, one large and the other small. Upon binding of the inhibitor, the small domain rotates by 5 degrees toward the large domain to close the active site. This domain movement is caused mainly by small but important main-chain conformational changes in the residues located over the domain interface of the small domain. In chicken mitochondrial AspAT, the domain movement was larger, with a rotational angle of 13 degrees. By comparison of these two structures, the difference in the rotational angles was found to be caused by the larger opening of the domain in the open form of chicken mitochondrial AspAT. Although the overall structures of these two enzymes were almost identical, the surface area of the domain interface in the E. coli enzyme was larger than that in mitochondrial AspAT, suggesting that the structure of the domain interface is responsible for the degree of movement of the small domain.

About this StructureAbout this Structure

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

ReferenceReference

X-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form., Okamoto A, Higuchi T, Hirotsu K, Kuramitsu S, Kagamiyama H, J Biochem. 1994 Jul;116(1):95-107. PMID:7798192 Page seeded by OCA on Fri May 2 10:37:46 2008

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

OCA

@@ Line 1: / Line 1: @@
 [[Image:1art.jpg|left|200px]]
- {{Structure
+<!--
-|PDB= 1art |SIZE=350|CAPTION= <scene name='initialview01'>1art</scene>, resolution 1.8&Aring;
+The line below this paragraph, containing "STRUCTURE_1art", 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=CH3:METHYL+GROUP'>CH3</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/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </span>
+or leave the SCENE parameter empty for the default display.
-|GENE=
+-->
-|DOMAIN=
+{{STRUCTURE_1art|  PDB=1art  |  SCENE=  }}
-|RELATEDENTRY=
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1art FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1art OCA], [http://www.ebi.ac.uk/pdbsum/1art PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1art RCSB]</span>
-}}
 '''X-RAY CRYSTALLOGRAPHIC STUDY OF PYRIDOXAL 5'-PHOSPHATE-TYPE ASPARTATE AMINOTRANSFERASES FROM ESCHERICHIA COLI IN OPEN AND CLOSED FORM'''
@@ Line 29: / Line 26: @@
 [[Category: Hirotsu, K.]]
 [[Category: Okamoto, A.]]
-[[Category: transferase(aminotransferase)]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:37:46 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:46:19 2008''